Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.

Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as advanced materials in biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology and material science, to name only a few fields. In all these applications, the final function depends on: (i) the specific mechanisms of protein aggregation, (ii) the hierarchical structure of the protein and peptide amyloids from the atomistic to mesoscopic length scales and (iii) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial). In this review, we will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality. We also highlight current advances in the design and synthesis of amyloid-based biological and functional materials and identify new potential fields in which amyloid-based structures promise new breakthroughs.

[1]  Meital Reches,et al.  Novel electrochemical biosensing platform using self-assembled peptide nanotubes. , 2005, Nano letters.

[2]  Giovanni Dietler,et al.  Understanding amyloid aggregation by statistical analysis of atomic force microscopy images. , 2010, Nature nanotechnology.

[3]  M. Mazzotti,et al.  Amyloid Templated Gold Aerogels , 2016, Advanced materials.

[4]  M. Goulian,et al.  Amyloid-DNA Composites of Bacterial Biofilms Stimulate Autoimmunity. , 2015, Immunity.

[5]  J. Danielsson,et al.  Functional features cause misfolding of the ALS-provoking enzyme SOD1 , 2009, Proceedings of the National Academy of Sciences.

[6]  R. Tanzi,et al.  Modulation of A beta adhesiveness and secretase site cleavage by zinc. , 1994, The Journal of biological chemistry.

[7]  H. Tian,et al.  Peptide self-assembly triggered by metal ions. , 2015, Chemical Society reviews.

[8]  Tuomas P. J. Knowles,et al.  Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading , 2016, Proceedings of the National Academy of Sciences.

[9]  J. V. van Hest,et al.  Self-assembly and polymerization of diacetylene-containing peptide amphiphiles in aqueous solution. , 2008, Biomacromolecules.

[10]  J. Rochet,et al.  α-Synuclein-induced tubule formation in lipid bilayers. , 2011, The journal of physical chemistry. B.

[11]  Tomonori Waku,et al.  Self-assembled β-Sheet Peptide Nanofibers for Efficient Antigen Delivery , 2013 .

[12]  M. Fändrich,et al.  Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity. , 2012, Journal of molecular biology.

[13]  Michele Vendruscolo,et al.  Atomic structure and hierarchical assembly of a cross-β amyloid fibril , 2013, Proceedings of the National Academy of Sciences.

[14]  R. Nanga,et al.  Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity , 2010, Proceedings of the National Academy of Sciences.

[15]  J. Danielsson,et al.  SOD1 aggregation in ALS mice shows simplistic test tube behavior , 2015, Proceedings of the National Academy of Sciences.

[16]  D. Topgaard,et al.  Membrane Lipid Co-Aggregation with α-Synuclein Fibrils , 2013, PloS one.

[17]  Zsofia Botyanszki,et al.  Programmable biofilm-based materials from engineered curli nanofibres , 2014, Nature Communications.

[18]  Tuomas P J Knowles,et al.  Amyloid Fibrils as Building Blocks for Natural and Artificial Functional Materials , 2016, Advanced materials.

[19]  D. Eisenberg,et al.  Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics. , 2011, Journal of the American Chemical Society.

[20]  J. Ávila,et al.  Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction , 1996 .

[21]  C. Dobson,et al.  Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.

[22]  R. Winter,et al.  Cold- and pressure-induced dissociation of protein aggregates and amyloid fibrils. , 2008, Angewandte Chemie.

[23]  Andreas Hoenger,et al.  De novo designed peptide-based amyloid fibrils , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[24]  Lei Liu,et al.  Size Effect of Graphene Oxide on Modulating Amyloid Peptide Assembly. , 2015, Chemistry.

[25]  Samuel I. Stupp,et al.  Nucleation and Growth of Ordered Arrays of Silver Nanoparticles on Peptide Nanofibers: Hybrid Nanostructures with Antimicrobial Properties , 2016, Journal of the American Chemical Society.

[26]  Bernard R Brooks,et al.  Influence of Nanoparticle Size and Shape on Oligomer Formation of an Amyloidogenic Peptide. , 2011, The journal of physical chemistry letters.

[27]  M. Molinari,et al.  In and out of the ER: protein folding, quality control, degradation, and related human diseases. , 2007, Physiological reviews.

[28]  R. Riek,et al.  Mechanism of membrane interaction and disruption by α-synuclein. , 2011, Journal of the American Chemical Society.

[29]  O. Inganäs,et al.  Integration of amyloid nanowires in organic solar cells , 2008 .

[30]  R. Sabaté,et al.  Amyloid-Like Protein Inclusions in Tobacco Transgenic Plants , 2010, PloS one.

[31]  Luqi Liu,et al.  Hierarchical Graphene‐Based Films with Dynamic Self‐Stiffening for Biomimetic Artificial Muscle , 2016 .

[32]  David Eisenberg,et al.  Atomic View of a Toxic Amyloid Small Oligomer , 2012, Science.

[33]  H. Levine,et al.  Thioflavine T interaction with synthetic Alzheimer's disease β‐amyloid peptides: Detection of amyloid aggregation in solution , 1993, Protein science : a publication of the Protein Society.

[34]  R. Marchant,et al.  ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures , 2004, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.

[35]  S. Sen,et al.  Self healing hydrogels composed of amyloid nano fibrils for cell culture and stem cell differentiation. , 2015, Biomaterials.

[36]  K. Kang,et al.  Mineralization of Self‐assembled Peptide Nanofibers for Rechargeable Lithium Ion Batteries , 2010, Advanced materials.

[37]  Mingzhen Zhang,et al.  Molecular understanding of a potential functional link between antimicrobial and amyloid peptides. , 2014, Soft matter.

[38]  H. Jaeger,et al.  Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[39]  R. Stephenson A and V , 1962, The British journal of ophthalmology.

[40]  Lei Zhao,et al.  TiO2 nanoparticles promote beta-amyloid fibrillation in vitro. , 2008, Biochemical and biophysical research communications.

[41]  A. Prescott,et al.  YuaB Functions Synergistically with the Exopolysaccharide and TasA Amyloid Fibers To Allow Biofilm Formation by Bacillus subtilis , 2011, Journal of bacteriology.

[42]  R. Mezzenga,et al.  Snapshots of fibrillation and aggregation kinetics in multistranded amyloid β-lactoglobulin fibrils , 2011 .

[43]  R. Mezzenga,et al.  Self-assembly of ovalbumin into amyloid and non-amyloid fibrils. , 2012, Biomacromolecules.

[44]  Michele Vendruscolo,et al.  Chemical kinetics for drug discovery to combat protein aggregation diseases. , 2014, Trends in pharmacological sciences.

[45]  A. Miranker,et al.  Fiber-dependent amyloid formation as catalysis of an existing reaction pathway , 2007, Proceedings of the National Academy of Sciences.

[46]  J. DiMaio,et al.  Coassembly of enantiomeric amphipathic peptides into amyloid-inspired rippled β-sheet fibrils. , 2012, Journal of the American Chemical Society.

[47]  R. Mezzenga,et al.  Freeze-Thaw Cycling Induced Isotropic-Nematic Coexistence of Amyloid Fibrils Suspensions. , 2016, Langmuir : the ACS journal of surfaces and colloids.

[48]  I. Hamley,et al.  Helical-ribbon formation by a beta-amino acid modified amyloid beta-peptide fragment. , 2009, Angewandte Chemie.

[49]  T. Kawai,et al.  Metal Ion-dependent Effects of Clioquinol on the Fibril Growth of an Amyloid β Peptide* , 2005, Journal of Biological Chemistry.

[50]  Maria Laura Bolognesi,et al.  Imaging of β-amyloid plaques by near infrared fluorescent tracers: a new frontier for chemical neuroscience. , 2015, Chemical Society reviews.

[51]  Daniela Kalafatovic,et al.  Exploring the sequence space for (tri-)peptide self-assembly to design and discover new hydrogels. , 2015, Nature chemistry.

[52]  W. Scheper,et al.  PEGylated nanoparticles bind to and alter amyloid-beta peptide conformation: toward engineering of functional nanomedicines for Alzheimer's disease. , 2012, ACS nano.

[53]  R. Boom,et al.  Peptides are building blocks of heat-induced fibrillar protein aggregates of beta-lactoglobulin formed at pH 2. , 2008, Biomacromolecules.

[54]  J. Danielsson,et al.  Ionic Strength Modulation of the Free Energy Landscape of Aβ40 Peptide Fibril Formation. , 2016, Journal of the American Chemical Society.

[55]  D. Price,et al.  Conservation of brain amyloid proteins in aged mammals and humans with Alzheimer's disease. , 1987, Science.

[56]  Jae Hong Kim,et al.  Self-assembled light-harvesting peptide nanotubes for mimicking natural photosynthesis. , 2012, Angewandte Chemie.

[57]  Ian W. Hamley,et al.  Hybrid Proton and Electron Transport in Peptide Fibrils , 2014 .

[58]  G. Howlett,et al.  Shear flow induces amyloid fibril formation. , 2006, Biomacromolecules.

[59]  I. Hamley,et al.  Self-assembling amphiphilic peptides , 2014, Journal of peptide science : an official publication of the European Peptide Society.

[60]  Jozef Adamcik,et al.  Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties. , 2012, Nature nanotechnology.

[61]  J. Karp,et al.  Nanocarriers as an Emerging Platform for Cancer Therapy , 2022 .

[62]  Krista L. Niece,et al.  Selective Differentiation of Neural Progenitor Cells by High-Epitope Density Nanofibers , 2004, Science.

[63]  I. Hamley Liquid crystal phase formation by biopolymers , 2010 .

[64]  Krista L. Niece,et al.  Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction. , 2003, Journal of the American Chemical Society.

[65]  Markus Rudin,et al.  In vivo detection of amyloid-β deposits by near-infrared imaging using an oxazine-derivative probe , 2005, Nature Biotechnology.

[66]  P. Schuck On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. , 2003, Analytical biochemistry.

[67]  K. Weber,et al.  Collagen network of the myocardium: function, structural remodeling and regulatory mechanisms. , 1994, Journal of molecular and cellular cardiology.

[68]  P. Zatta Metal Ions and Neurodegenerative Disorders , 2003 .

[69]  Massimo Morbidelli,et al.  Population balance modeling of antibodies aggregation kinetics. , 2012, The journal of physical chemistry. B.

[70]  J. D. Robertson,et al.  Copper, iron and zinc in Alzheimer's disease senile plaques , 1998, Journal of the Neurological Sciences.

[71]  S. Ribeiro,et al.  Immunosensor for diagnosis of Alzheimer disease using amyloid-β 1-40 peptide and silk fibroin thin films. , 2016, Materials science & engineering. C, Materials for biological applications.

[72]  Andrew G. Glen,et al.  APPL , 2001 .

[73]  Michele Vendruscolo,et al.  Molecular mechanisms of protein aggregation from global fitting of kinetic models , 2016, Nature Protocols.

[74]  S. Gras,et al.  Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading. , 2011, Biomaterials.

[75]  Samuel I Stupp,et al.  Peptide-amphiphile nanofibers: A versatile scaffold for the preparation of self-assembling materials , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[76]  Mi Zhou,et al.  Self-assembled peptide-based hydrogels as scaffolds for anchorage-dependent cells. , 2009, Biomaterials.

[77]  J. Lim,et al.  Dimethyl Sulfoxide and Ethanol Elicit Increased Amyloid Biogenesis and Amyloid-Integrated Biofilm Formation in Escherichia coli , 2012, Applied and Environmental Microbiology.

[78]  Michele Vendruscolo,et al.  The molecular chaperone Brichos breaks the catalytic cycle that generates toxic Aβ oligomers , 2015, Nature Structural &Molecular Biology.

[79]  R. de Vries,et al.  Strong impact of ionic strength on the kinetics of fibrilar aggregation of bovine beta-lactoglobulin. , 2006, Biomacromolecules.

[80]  Li Di,et al.  High throughput artificial membrane permeability assay for blood-brain barrier. , 2003, European journal of medicinal chemistry.

[81]  Shujuan Fan,et al.  Curcumin-conjugated magnetic nanoparticles for detecting amyloid plaques in Alzheimer's disease mice using magnetic resonance imaging (MRI). , 2015, Biomaterials.

[82]  Yves F Dufrêne,et al.  Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide. , 2009, The Biochemical journal.

[83]  Alexander K. Buell,et al.  Probing small molecule binding to amyloid fibrils. , 2011, Physical chemistry chemical physics : PCCP.

[84]  R. Bitton,et al.  The role of nanoscale architecture in supramolecular templating of biomimetic hydroxyapatite mineralization. , 2012, Small.

[85]  S. Radford,et al.  Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro. , 2000, Biochemistry.

[86]  Mark A. Smith,et al.  In Situ Oxidative Catalysis by Neurofibrillary Tangles and Senile Plaques in Alzheimer’s Disease , 2000, Journal of neurochemistry.

[87]  R. Losick,et al.  Amyloid fibers provide structural integrity to Bacillus subtilis biofilms , 2010, Proceedings of the National Academy of Sciences.

[88]  Clemens F. Kaminski,et al.  Direct Observation of Heterogeneous Amyloid Fibril Growth Kinetics via Two-Color Super-Resolution Microscopy , 2013, Nano letters.

[89]  R. Mezzenga,et al.  Nematic field transfer in a two-dimensional protein fibril assembly. , 2016, Soft matter.

[90]  S. Radford,et al.  An imaging and systems modeling approach to fibril breakage enables prediction of amyloid behavior. , 2013, Biophysical journal.

[91]  C. L. Teoh,et al.  Bovine serum albumin unfolds in Couette flow , 2012 .

[92]  Meital Reches,et al.  Peptide nanotube-modified electrodes for enzyme-biosensor applications. , 2005, Analytical chemistry.

[93]  E. Linden,et al.  Self-assembly and aggregation of proteins , 2007 .

[94]  J. M. Lage 100 Years of Alzheimer's disease (1906-2006). , 2006, Journal of Alzheimer's disease : JAD.

[95]  M. Tena-Solsona,et al.  Co-assembly of tetrapeptides into complex pH-responsive molecular hydrogel networks. , 2014, Journal of materials chemistry. B.

[96]  Kory Jenkins,et al.  Self-assembly of diphenylalanine peptide with controlled polarization for power generation , 2016, Nature Communications.

[97]  W. Klein,et al.  Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5 , 2010, Neuron.

[98]  C. Masters,et al.  Rapid induction of Alzheimer A beta amyloid formation by zinc. , 1994, Science.

[99]  J. Sugiyama,et al.  Morphology control between twisted ribbon, helical ribbon, and nanotube self-assemblies with his-containing helical peptides in response to pH change. , 2014, Langmuir.

[100]  O. Inganäs,et al.  Enhanced current efficiency from bio-organic light-emitting diodes using decorated amyloid fibrils with conjugated polymer. , 2008, Nano letters.

[101]  S. Radford,et al.  Nucleation of protein fibrillation by nanoparticles , 2007, Proceedings of the National Academy of Sciences.

[102]  Michele Vendruscolo,et al.  Metastability of native proteins and the phenomenon of amyloid formation. , 2011, Journal of the American Chemical Society.

[103]  R. Mezzenga,et al.  Direct observation of time-resolved polymorphic states in the self-assembly of end-capped heptapeptides. , 2011, Angewandte Chemie.

[104]  T. Härd,et al.  Amyloid Fibrils: Formation, Polymorphism, and Inhibition. , 2014, The journal of physical chemistry letters.

[105]  A. Bush,et al.  Metals and Alzheimer's disease. , 2006, Journal of Alzheimer's disease : JAD.

[106]  Fabrication of amyloid peptide micro‐arrays using laser‐induced forward transfer and avidin‐biotin mediated assembly , 2008 .

[107]  O. Inganäs,et al.  Preparation of phosphorescent amyloid-like protein fibrils. , 2010, Chemistry.

[108]  Sergei V. Kalinin,et al.  Double-layer mediated electromechanical response of amyloid fibrils in liquid environment. , 2010, ACS nano.

[109]  L. A. Lane,et al.  Enhanced Detection Specificity and Sensitivity of Alzheimer's Disease Using Amyloid-β-Targeted Quantum Dots. , 2016, Bioconjugate chemistry.

[110]  J. Gerrard,et al.  Stability and cytotoxicity of crystallin amyloid nanofibrils. , 2014, Nanoscale.

[111]  K. Jandt,et al.  Controlled self-assembly and templated metallization of fibrinogen nanofibrils. , 2008, Chemical communications.

[112]  K. Yung,et al.  N-Acetyl-l-cysteine capped quantum dots offer neuronal cell protection by inhibiting beta (1-40) amyloid fibrillation. , 2013, Biomaterials science.

[113]  A. Bush,et al.  Metals and neuroscience. , 2000, Current opinion in chemical biology.

[114]  E. Placidi,et al.  Self-assembly of a model peptide incorporating a hexa-histidine sequence attached to an oligo-alanine sequence, and binding to gold NTA/nickel nanoparticles. , 2014, Biomacromolecules.

[115]  D. Eisenberg,et al.  Designed amyloid fibers as materials for selective carbon dioxide capture , 2013, Proceedings of the National Academy of Sciences.

[116]  A. Steven,et al.  Membrane Curvature Induction and Tubulation Are Common Features of Synucleins and Apolipoproteins* , 2010, The Journal of Biological Chemistry.

[117]  H. Cui,et al.  One-Component Supramolecular Filament Hydrogels as Theranostic Label-Free Magnetic Resonance Imaging Agents. , 2017, ACS nano.

[118]  C. Robinson,et al.  Removal of the N‐terminal hexapeptide from human β2‐microglobulin facilitates protein aggregation and fibril formation , 2000, Protein science : a publication of the Protein Society.

[119]  J. Brodin,et al.  Designed, Helical Protein Nanotubes with Variable Diameters from a Single Building Block. , 2015, Journal of the American Chemical Society.

[120]  A. Steven,et al.  α-Synuclein Amyloid Fibrils with Two Entwined, Asymmetrically Associated Protofibrils* , 2015, The Journal of Biological Chemistry.

[121]  G. Perry,et al.  Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[122]  Earl J. Bergey,et al.  Organically Modified Silica Nanoparticles Are Biocompatible and Can Be Targeted to Neurons In Vivo , 2012, PloS one.

[123]  R. Mezzenga,et al.  Polymorphism complexity and handedness inversion in serum albumin amyloid fibrils. , 2013, ACS nano.

[124]  J. Pettegrew,et al.  Alzheimer’s Disease: Soluble Oligomeric Aβ(1–40) Peptide in Membrane Mimic Environment from Solution NMR and Circular Dichroism Studies , 2004, Neurochemical Research.

[125]  R. Zhou,et al.  Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides. , 2014, Nanoscale.

[126]  R. Mezzenga,et al.  Modulating Materials by Orthogonally Oriented β‐Strands: Composites of Amyloid and Silk Fibroin Fibrils , 2014, Advanced materials.

[127]  S. Burgard ISR , 1999 .

[128]  D. Dunstan,et al.  Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils , 2009 .

[129]  Sreenath Bolisetty,et al.  Amyloid-carbon hybrid membranes for universal water purification. , 2016, Nature nanotechnology.

[130]  Michele Vendruscolo,et al.  An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer’s disease , 2016, Science Advances.

[131]  S. King,et al.  Self-assembly of Peptide nanotubes in an organic solvent. , 2008, Langmuir : the ACS journal of surfaces and colloids.

[132]  P. Kinnunen,et al.  The role of lipid-protein interactions in amyloid-type protein fibril formation. , 2006, Chemistry and physics of lipids.

[133]  Jason T Giurleo,et al.  In vitro formation of amyloid from alpha-synuclein is dominated by reactions at hydrophobic interfaces. , 2010, Journal of the American Chemical Society.

[134]  Jun Hu,et al.  Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier , 2015, Proceedings of the National Academy of Sciences.

[135]  Ian W. Hamley,et al.  Multiwalled Nanotubes Formed by Catanionic Mixtures of Drug Amphiphiles , 2014, ACS nano.

[136]  M. Biancalana,et al.  Molecular mechanism of Thioflavin-T binding to amyloid fibrils. , 2010, Biochimica et biophysica acta.

[137]  A. Kelarakis,et al.  Self-assembly and hydrogelation of an amyloid peptide fragment. , 2008, Biochemistry.

[138]  Shiri Stempler,et al.  Self-assembled arrays of peptide nanotubes by vapour deposition. , 2009, Nature nanotechnology.

[139]  P. Lansbury,et al.  Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. , 2002, Biochemistry.

[140]  Christopher J Roberts,et al.  A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding. , 2007, The journal of physical chemistry. B.

[141]  Ehud Gazit,et al.  Fabrication of coaxial metal nanocables using a self-assembled peptide nanotube scaffold. , 2006, Nano letters.

[142]  Xudong Huang,et al.  Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis* , 1998, The Journal of Biological Chemistry.

[143]  S. Gras,et al.  Bioactive TTR105-115-based amyloid fibrils reduce the viability of mammalian cells. , 2015, Biomaterials.

[144]  C. Rienstra,et al.  Structural intermediates during α-synuclein fibrillogenesis on phospholipid vesicles. , 2012, Journal of the American Chemical Society.

[145]  Yousef M. Abul-Haija,et al.  Pickering stabilized peptide gel particles as tunable microenvironments for biocatalysis. , 2013, Langmuir : the ACS journal of surfaces and colloids.

[146]  I. Hamley,et al.  New Self-Assembling Multifunctional Templates for the Biofabrication and Controlled Self-Release of Cultured Tissue , 2015, Tissue engineering. Part A.

[147]  M. Muschol,et al.  Amyloid Oligomers and Protofibrils, but Not Filaments, Self-Replicate from Native Lysozyme , 2014, Journal of the American Chemical Society.

[148]  K. E. Styan,et al.  Nanotopographic surfaces with defined surface chemistries from amyloid fibril networks can control cell attachment. , 2013, Biomacromolecules.

[149]  S. Linse,et al.  Effects of Polyamino Acids and Polyelectrolytes on Amyloid β Fibril Formation , 2014, Langmuir : the ACS journal of surfaces and colloids.

[150]  M. Morbidelli,et al.  Kinetic analysis of the multistep aggregation mechanism of monoclonal antibodies. , 2014, The journal of physical chemistry. B.

[151]  F. Hartl,et al.  Converging concepts of protein folding in vitro and in vivo , 2009, Nature Structural &Molecular Biology.

[152]  R. Mezzenga,et al.  Liquid crystalline phase behavior of protein fibers in water: experiments versus theory. , 2010, Langmuir : the ACS journal of surfaces and colloids.

[153]  R. Mezzenga,et al.  Gelation, phase behavior, and dynamics of β-lactoglobulin amyloid fibrils at varying concentrations and ionic strengths. , 2012, Biomacromolecules.

[154]  Sebastian Maurer-Stroh,et al.  Amyloid-based nanosensors and nanodevices. , 2014, Chemical Society reviews.

[155]  E. Gazit,et al.  Self-organization of Short Peptide Fragments: From Amyloid Fibrils to Nanoscale Supramolecular Assemblies , 2005 .

[156]  Tuomas P. J. Knowles,et al.  Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide , 2016, Scientific Reports.

[157]  Kevin Barraclough,et al.  I and i , 2001, BMJ : British Medical Journal.

[158]  H. Naiki,et al.  Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils , 2009, Proceedings of the National Academy of Sciences.

[159]  W. Alves,et al.  Structural behaviour and gene delivery in complexes formed between DNA and arginine-containing peptide amphiphiles. , 2016, Soft matter.

[160]  Mehmet Sarikaya,et al.  Selective detection of target proteins by peptide-enabled graphene biosensor. , 2014, Small.

[161]  Markus J Buehler,et al.  Nanomechanics of functional and pathological amyloid materials. , 2011, Nature nanotechnology.

[162]  Meital Reches,et al.  Amyloid Fibril Formation by Pentapeptide and Tetrapeptide Fragments of Human Calcitonin* , 2002, The Journal of Biological Chemistry.

[163]  I. Hamley,et al.  Self-assembled arginine-coated peptide nanosheets in water. , 2013, Chemical communications.

[164]  D. Otzen,et al.  Amyloid adhesins are abundant in natural biofilms. , 2007, Environmental microbiology.

[165]  G. Fuller,et al.  Quantitative analysis of amyloid-integrated biofilms formed by uropathogenic Escherichia coli at the air-liquid interface. , 2012, Biophysical journal.

[166]  Mathew H Horrocks,et al.  A mechanistic model of tau amyloid aggregation based on direct observation of oligomers , 2015, Nature Communications.

[167]  David R. Brown Brain proteins that mind metals: a neurodegenerative perspective. , 2009, Dalton transactions.

[168]  Yun-Ru Chen,et al.  Negatively charged gold nanoparticles inhibit Alzheimer's amyloid-β fibrillization, induce fibril dissociation, and mitigate neurotoxicity. , 2012, Small.

[169]  R. Mezzenga,et al.  ILQINS hexapeptide, identified in lysozyme left-handed helical ribbons and nanotubes, forms right-handed helical ribbons and crystals. , 2014, Journal of the American Chemical Society.

[170]  E. Gazit,et al.  Self-assembly of peptide nanotubes and amyloid-like structures by charged-termini-capped diphenylalanine peptide analogues , 2005 .

[171]  B. Nordén,et al.  Multiphoton absorption in amyloid protein fibres , 2013, Nature Photonics.

[172]  S. Gras,et al.  Biomimetic topography and chemistry control cell attachment to amyloid fibrils. , 2015, Biomacromolecules.

[173]  T. Morgan,et al.  Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[174]  K. Jandt,et al.  Novel 1-D biophotonic nanohybrids: protein nanofibers meet quantum dots , 2011 .

[175]  M. Smith,et al.  Redox metals and neurodegenerative disease. , 1999, Current opinion in chemical biology.

[176]  Y. Ko,et al.  Amyloid β oligomerization is induced by brain lipid rafts , 2006 .

[177]  C. Ionescu-Zanetti,et al.  Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. , 2001, Biochemistry.

[178]  D. Selkoe,et al.  Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide , 2007, Nature Reviews Molecular Cell Biology.

[179]  C. MacPhee,et al.  Efficient energy transfer within self-assembling peptide fibers: a route to light-harvesting nanomaterials. , 2009, Journal of the American Chemical Society.

[180]  I. Hamley Amyloid formation: Interface influence. , 2010, Nature chemistry.

[181]  Jin Gu,et al.  2D Protein Supramolecular Nanofilm with Exceptionally Large Area and Emergent Functions , 2016, Advanced materials.

[182]  Christopher M. Dobson,et al.  Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein , 2012, Cell.

[183]  Alexander K. Buell,et al.  The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation. , 2014, Journal of the American Chemical Society.

[184]  T. Jovin,et al.  Quantum dots as ultrasensitive nanoactuators and sensors of amyloid aggregation in live cells. , 2009, Journal of the American Chemical Society.

[185]  M. Fändrich,et al.  Structure and biomedical applications of amyloid oligomer nanoparticles. , 2014, ACS nano.

[186]  Dong Men,et al.  Integration of a fluorescent molecular biosensor into self-assembled protein nanowires: a large sensitivity enhancement. , 2010, Angewandte Chemie.

[187]  S. Linse,et al.  The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate , 2011, Langmuir : the ACS journal of surfaces and colloids.

[188]  P. Lansbury,et al.  Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[189]  H. Dyson,et al.  Intrinsically unstructured proteins and their functions , 2005, Nature Reviews Molecular Cell Biology.

[190]  Peter Fischer,et al.  The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions , 2013, Reports on progress in physics. Physical Society.

[191]  Sara Linse,et al.  Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. , 2007, Angewandte Chemie.

[192]  Paramjit S. Arora,et al.  Amyloid fibrils nucleated and organized by DNA origami constructions , 2014, Nature nanotechnology.

[193]  R. Mezzenga,et al.  Adjustable twisting periodic pitch of amyloid fibrils , 2011 .

[194]  P. Lansbury,et al.  Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. , 2000, Biochemistry.

[195]  Glyn L. Devlin,et al.  Functionalised amyloid fibrils for roles in cell adhesion. , 2008, Biomaterials.

[196]  Thomas C T Michaels,et al.  Dynamics of protein aggregation and oligomer formation governed by secondary nucleation. , 2015, The Journal of chemical physics.

[197]  Frank Heinrich,et al.  Depth of α-synuclein in a bilayer determined by fluorescence, neutron reflectometry, and computation. , 2012, Biophysical journal.

[198]  D. Nochlin,et al.  The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease. , 1988, The American journal of pathology.

[199]  J. Bernhagen,et al.  Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. , 2000, Journal of molecular biology.

[200]  S. Habelitz,et al.  Amyloid-like ribbons of amelogenins in enamel mineralization , 2016, Scientific Reports.

[201]  Juan J de Pablo,et al.  Structural motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy , 2014, Proceedings of the National Academy of Sciences.

[202]  Jin-Mi Jung,et al.  Interfacial activity and interfacial shear rheology of native β-lactoglobulin monomers and their heat-induced fibers. , 2010, Langmuir : the ACS journal of surfaces and colloids.

[203]  P. Messersmith,et al.  Seamless Metallic Coating and Surface Adhesion of Self-Assembled Bioinspired Nanostructures Based on Di-(3,4-dihydroxy-l-phenylalanine) Peptide Motif , 2014, ACS nano.

[204]  Thomas Arnold,et al.  Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives , 2017, Scientific Reports.

[205]  T. Ban,et al.  Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability. , 2005, Biochemistry.

[206]  C. Dobson,et al.  Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements. , 2008, Angewandte Chemie.

[207]  L. Wyns,et al.  Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic β2-microglobulin variant , 2011, Proceedings of the National Academy of Sciences of the United States of America.

[208]  Yifan Cheng,et al.  Self-aligning amelogenin nanoribbons in oil-water system. , 2011, Journal of structural biology.

[209]  S. Dante,et al.  Membrane fusogenic activity of the Alzheimer's peptide A beta(1-42) demonstrated by small-angle neutron scattering. , 2008, Journal of molecular biology.

[210]  A. Corrigan,et al.  The formation of nematic liquid crystal phases by hen lysozyme amyloid fibrils. , 2006, Journal of the American Chemical Society.

[211]  J. H. Viles,et al.  Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases , 2012 .

[212]  D. Dickson,et al.  Dimeric Amyloid β Protein Rapidly Accumulates in Lipid Rafts followed by Apolipoprotein E and Phosphorylated Tau Accumulation in the Tg2576 Mouse Model of Alzheimer's Disease , 2004, The Journal of Neuroscience.

[213]  Alexander K. Buell,et al.  Detailed analysis of the energy barriers for amyloid fibril growth. , 2012, Angewandte Chemie.

[214]  Jae Hong Kim,et al.  Self-Assembly of Metalloporphyrins into Light-Harvesting Peptide Nanofiber Hydrogels for Solar Water Oxidation , 2014 .

[215]  Alexander K. Buell,et al.  Nanostructured films from hierarchical self-assembly of amyloidogenic proteins. , 2010, Nature nanotechnology.

[216]  JoAnne McLaurin,et al.  Small molecule inhibitors of Aβ‐aggregation and neurotoxicity , 2009 .

[217]  R. Mezzenga,et al.  General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons. , 2011, Biomacromolecules.

[218]  R. Mezzenga,et al.  Proteins Fibrils from a Polymer Physics Perspective , 2012 .

[219]  S. Radford,et al.  Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis , 2009, Protein engineering, design & selection : PEDS.

[220]  J. Castle,et al.  Transformation of amyloid-like fibers, formed from an elastin-based biopolymer, into a hydrogel: an X-ray photoelectron spectroscopy and atomic force microscopy study. , 2007, Biomacromolecules.

[221]  A. Miu,et al.  Aluminum and Alzheimer's disease: a new look. , 2006, Journal of Alzheimer's disease : JAD.

[222]  C. L. Teoh,et al.  Apolipoproteins and amyloid fibril formation in atherosclerosis , 2011, Protein & Cell.

[223]  K. Schwarz,et al.  Peptide nanofibrils boost retroviral gene transfer and provide a rapid means for concentrating viruses. , 2013, Nature nanotechnology.

[224]  O. Inganäs,et al.  White light with phosphorescent protein fibrils in OLEDs. , 2010, Nano letters.

[225]  Jie Li,et al.  The Association of α-Synuclein with Membranes Affects Bilayer Structure, Stability, and Fibril Formation* , 2003, Journal of Biological Chemistry.

[226]  Wei Liu,et al.  Collagen Tissue Engineering: Development of Novel Biomaterials and Applications , 2008, Pediatric Research.

[227]  H. Möhwald,et al.  Uniaxially oriented peptide crystals for active optical waveguiding. , 2011, Angewandte Chemie.

[228]  D. Lamprou,et al.  Beta-adrenoceptor antagonists affect amyloid nanostructure; amyloid hydrogels as drug delivery vehicles. , 2013, Chemical communications.

[229]  Sara Linse,et al.  Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides , 2014, Proceedings of the National Academy of Sciences.

[230]  Nicholas Stephanopoulos,et al.  The Powerful Functions of Peptide-Based Bioactive Matrices for Regenerative Medicine , 2014, Annals of Biomedical Engineering.

[231]  S. Linse,et al.  Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation. , 2016, Analytical biochemistry.

[232]  K. Sörgjerd,et al.  Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. , 2007, Journal of molecular biology.

[233]  B. Penke,et al.  Functionalization of gold nanoparticles with amino acid, beta-amyloid peptides and fragment. , 2010, Colloids and surfaces. B, Biointerfaces.

[234]  Ehud Gazit,et al.  Self-assembly of short peptides to form hydrogels: design of building blocks, physical properties and technological applications. , 2014, Acta biomaterialia.

[235]  C. Dobson,et al.  Fast flow microfluidics and single-molecule fluorescence for the rapid characterization of α-synuclein oligomers. , 2015, Analytical chemistry.

[236]  C. Masters,et al.  Aqueous Dissolution of Alzheimer’s Disease Aβ Amyloid Deposits by Biometal Depletion* , 1999, The Journal of Biological Chemistry.

[237]  R. Mezzenga,et al.  Amyloid fibrils enhance transport of metal nanoparticles in living cells and induced cytotoxicity. , 2014, Biomacromolecules.

[238]  L. Serpell,et al.  Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly:  implications for amyloid fibril formation and materials science. , 2000, Journal of the American Chemical Society.

[239]  R. Mezzenga,et al.  Hybrid Nanocomposites of Gold Single‐Crystal Platelets and Amyloid Fibrils with Tunable Fluorescence, Conductivity, and Sensing Properties , 2013, Advanced materials.

[240]  C. Finch,et al.  Self-assembly of Aβ1-42 into globular neurotoxins , 2003 .

[241]  A. Donald,et al.  Mechanisms of structure formation in particulate gels of β-lactoglobulin formed near the isoelectric point , 2006, The European physical journal. E, Soft matter.

[242]  V. Subramaniam,et al.  Dependence of α-synuclein aggregate morphology on solution conditions , 2002 .

[243]  Tuomas P. J. Knowles,et al.  An Analytical Solution to the Kinetics of Breakable Filament Assembly , 2009, Science.

[244]  L. Cegelski,et al.  Congo Red Interactions with Curli-Producing E. coli and Native Curli Amyloid Fibers , 2015, PloS one.

[245]  V. Uversky,et al.  Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. , 2001, Biochemistry.

[246]  Meital Reches,et al.  Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes , 2003, Science.

[247]  R. Mezzenga,et al.  Engineered lysozyme amyloid fibril networks support cellular growth and spreading. , 2014, Biomacromolecules.

[248]  L. Liz‐Marzán,et al.  Nucleation of Amyloid Oligomers by RepA-WH1-Prionoid-Functionalized Gold Nanorods. , 2016, Angewandte Chemie.

[249]  C. Degueldre,et al.  Offline Persistence of Memory-Related Cerebral Activity during Active Wakefulness , 2006, PLoS biology.

[250]  Gang Wei,et al.  Sequence‐Designed Peptide Nanofibers Bridged Conjugation of Graphene Quantum Dots with Graphene Oxide for High Performance Electrochemical Hydrogen Peroxide Biosensor , 2017 .

[251]  L. Domigan,et al.  Versatile multi-functionalization of protein nanofibrils for biosensor applications. , 2014, Nanoscale.

[252]  X. Qu,et al.  Polyoxometalates as inhibitors of the aggregation of amyloid β peptides associated with Alzheimer's disease. , 2011, Angewandte Chemie.

[253]  L. Bi,et al.  An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing. , 2010, Biosensors & bioelectronics.

[254]  B. Reif,et al.  A Hot-Segment-Based Approach for the Design of Cross-Amyloid Interaction Surface Mimics as Inhibitors of Amyloid Self-Assembly. , 2015, Angewandte Chemie.

[255]  R. Mezzenga,et al.  Universal behavior in the mesoscale properties of amyloid fibrils. , 2014, Physical review letters.

[256]  Sara Linse,et al.  Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process. , 2010, ACS chemical neuroscience.

[257]  A. Alexandrescu,et al.  pH dependence of amylin fibrillization. , 2014, Biochemistry.

[258]  G. J. Raymond,et al.  The most infectious prion protein particles , 2005, Nature.

[259]  K. Kang,et al.  Synthesis of diphenylalanine/cobalt oxide hybrid nanowires and their application to energy storage. , 2010, ACS nano.

[260]  H. Möhwald,et al.  Self‐Assembly of Hexagonal Peptide Microtubes and Their Optical Waveguiding , 2011, Advanced materials.

[261]  C. MacPhee,et al.  Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops. , 2000, Biochemistry.

[262]  N. Kotov,et al.  Inhibition of amyloid peptide fibrillation by inorganic nanoparticles: functional similarities with proteins. , 2011, Angewandte Chemie.

[263]  Martin M. F. Choi,et al.  Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-L-cysteine capped quantum dots. , 2010, Biomaterials.

[264]  H. Levine Quantification of beta-sheet amyloid fibril structures with thioflavin T. , 1999, Methods in enzymology.

[265]  K. Jandt,et al.  Novel biopolymeric template for the nucleation and growth of hydroxyapatite crystals based on self-assembled fibrinogen fibrils. , 2008, Biomacromolecules.

[266]  Young-Ho Lee,et al.  Cold denaturation of α-synuclein amyloid fibrils. , 2014, Angewandte Chemie.

[267]  Ehud Gazit,et al.  The "Correctly Folded" state of proteins: is it a metastable state? , 2002, Angewandte Chemie.

[268]  R. Riek,et al.  Amyloid as a Depot for the Formulation of Long-Acting Drugs , 2008, PLoS biology.

[269]  W. Marsden I and J , 2012 .

[270]  J. Parquette,et al.  A pi-conjugated hydrogel based on an Fmoc-dipeptide naphthalene diimide semiconductor. , 2010, Chemical communications.

[271]  A. Alexandrescu,et al.  Hydrogen exchange of monomeric α‐synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli , 2008, Protein science : a publication of the Protein Society.

[272]  J. Kelly,et al.  The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. , 1998, Current opinion in structural biology.

[273]  R. Kayed,et al.  Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer* , 2009, Journal of Biological Chemistry.

[274]  V. Martorana,et al.  Kinetics of insulin aggregation: disentanglement of amyloid fibrillation from large-size cluster formation. , 2006, Biophysical journal.

[275]  Matthew R Chapman,et al.  Diversity, biogenesis and function of microbial amyloids. , 2012, Trends in microbiology.

[276]  K. Kar,et al.  Evidence of rapid coaggregation of globular proteins during amyloid formation. , 2014, Biochemistry.

[277]  Ehud Gazit,et al.  Amyloids: not only pathological agents but also ordered nanomaterials. , 2008, Angewandte Chemie.

[278]  M. Morbidelli,et al.  A Colloidal Description of Intermolecular Interactions Driving Fibril-Fibril Aggregation of a Model Amphiphilic Peptide. , 2015, Langmuir : the ACS journal of surfaces and colloids.

[279]  Tomonori Waku,et al.  Recent advances in nanofibrous assemblies based on β‐sheet‐forming peptides for biomedical applications , 2017 .

[280]  P. Björk,et al.  Electroactive Luminescent Self‐Assembled Bio‐organic Nanowires: Integration of Semiconducting Oligoelectrolytes within Amyloidogenic Proteins , 2005 .

[281]  H. Saji,et al.  A (68)Ga complex based on benzofuran scaffold for the detection of β-amyloid plaques. , 2014, Bioorganic & medicinal chemistry letters.

[282]  G. Brezesinski,et al.  Triggers for β-sheet formation at the hydrophobic-hydrophilic interface: high concentration, in-plane orientational order, and metal ion complexation. , 2011, Langmuir : the ACS journal of surfaces and colloids.

[283]  Derek N. Woolfson,et al.  Rational design and application of responsive α-helical peptide hydrogels , 2009, Nature materials.

[284]  R. Mezzenga,et al.  Towards lysozyme nanotube and 3D hybrid self-assembly. , 2013, Nanoscale.

[285]  M. Dong,et al.  2D-oriented self-assembly of peptides induced by hydrated electrons. , 2012, Chemistry.

[286]  M. Welland,et al.  Conducting core-shell nanowires by amyloid nanofiber templated polymerization. , 2015, Biomacromolecules.

[287]  D. Otzen,et al.  Coexistence of ribbon and helical fibrils originating from hIAPP20–29 revealed by quantitative nanomechanical atomic force microscopy , 2013, Proceedings of the National Academy of Sciences.

[288]  K. P. Murphy,et al.  Common features of protein unfolding and dissolution of hydrophobic compounds. , 1990, Science.

[289]  Eunji Lee,et al.  The HA-incorporated nanostructure of a peptide-drug amphiphile for targeted anticancer drug delivery. , 2016, Chemical communications.

[290]  R. Mezzenga,et al.  Fibrillation of β-lactoglobulin at low pH in the presence of a complexing anionic polysaccharide. , 2010, Langmuir : the ACS journal of surfaces and colloids.

[291]  S. Kim,et al.  Liquid Crystalline Peptide Nanowires , 2007 .

[292]  Chan Beum Park,et al.  Photoluminescent Peptide Nanotubes , 2009 .

[293]  A. Banerjee,et al.  Short peptide based hydrogels: incorporation of graphene into the hydrogel , 2011 .

[294]  Jonathan A. Jones,et al.  The circularization of amyloid fibrils formed by apolipoprotein C-II. , 2003, Biophysical journal.

[295]  D. Raleigh,et al.  Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects. , 2012, Biochemistry.

[296]  Aaas News,et al.  Book Reviews , 1893, Buffalo Medical and Surgical Journal.

[297]  Xian‐Zheng Zhang,et al.  Hierarchical self-assembly of a β-amyloid peptide derivative. , 2013, Journal of materials chemistry. B.

[298]  Sara Linse,et al.  Inhibition of amyloid beta protein fibrillation by polymeric nanoparticles. , 2008, Journal of the American Chemical Society.

[299]  E. Opie THE RELATION OE DIABETES MELLITUS TO LESIONS OF THE PANCREAS. HYALINE DEGENERATION OF THE ISLANDS OE LANGERHANS , 1901, The Journal of experimental medicine.

[300]  Q. Luo,et al.  Protein Assembly: Versatile Approaches to Construct Highly Ordered Nanostructures. , 2016, Chemical reviews.

[301]  Roland Winter,et al.  Cross-amyloid interaction of Aβ and IAPP at lipid membranes. , 2012, Angewandte Chemie.

[302]  P. Fraser,et al.  Review: Modulating Factors in Amyloid-β Fibril Formation , 2000 .

[303]  Yves F. Dufrêne,et al.  A Role for Amyloid in Cell Aggregation and Biofilm Formation , 2011, PloS one.

[304]  Manuel Théry,et al.  Actin Network Architecture Can Determine Myosin Motor Activity , 2012, Science.

[305]  Vincenzo Martorana,et al.  Aggregation of a multidomain protein: A coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress , 2010, Protein science : a publication of the Protein Society.

[306]  Sunghyun Cho,et al.  Amyloid hydrogel derived from curly protein fibrils of alpha-synuclein. , 2010, Biomaterials.

[307]  D. Pochan,et al.  Rheological properties of peptide-based hydrogels for biomedical and other applications. , 2010, Chemical Society reviews.

[308]  P. Venema,et al.  Investigating the permanent electric dipole moment of β‐lactoglobulin fibrils, using transient electric birefringence , 2006, Biopolymers.

[309]  P. Schuck,et al.  Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. , 2000, Biophysical journal.

[310]  R. Mezzenga,et al.  Sol-gel transition of charged fibrils composed of a model amphiphilic peptide. , 2015, Journal of colloid and interface science.

[311]  R. Mezzenga,et al.  Inhibiting, promoting, and preserving stability of functional protein fibrils , 2012 .

[312]  C. Dobson,et al.  Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation , 2015, Proceedings of the National Academy of Sciences.

[313]  R. Riek,et al.  The presence of an air-water interface affects formation and elongation of α-Synuclein fibrils. , 2014, Journal of the American Chemical Society.

[314]  Christopher J Roberts,et al.  Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies. , 2010, Journal of pharmaceutical sciences.

[315]  A. Doig,et al.  Inhibition of protein aggregation and amyloid formation by small molecules. , 2015, Current opinion in structural biology.

[316]  T. Lu,et al.  Strong underwater adhesives made by self-assembling multi-protein nanofibres. , 2014, Nature nanotechnology.

[317]  R. Pappu,et al.  A polymer physics perspective on driving forces and mechanisms for protein aggregation. , 2008, Archives of biochemistry and biophysics.

[318]  M. Rowan,et al.  Amyloid Oligomers and Mature Fibrils Prepared from an Innocuous Protein Cause Diverging Cellular Death Mechanisms* , 2015, The Journal of Biological Chemistry.

[319]  P. Fraser,et al.  Effects of Sulfate Ions on Alzheimer β/A4 Peptide Assemblies: Implications for Amyloid Fibril‐Proteoglycan Interactions , 1992, Journal of neurochemistry.

[320]  Xiaochen Wu,et al.  Amyloid-graphene oxide as immobilization platform of Au nanocatalysts and enzymes for improved glucose-sensing activity. , 2017, Journal of colloid and interface science.

[321]  I. Lasa,et al.  Amyloid Structures as Biofilm Matrix Scaffolds , 2016, Journal of bacteriology.

[322]  G. Rivas,et al.  Analytical ultracentrifugation for the study of protein association and assembly. , 2006, Current opinion in chemical biology.

[323]  R. Mezzenga,et al.  The effect of pH on the self-assembly of a collagen derived peptide amphiphile , 2013 .

[324]  M. Maeda,et al.  Formation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin , 2008, The FEBS journal.

[325]  Roland Riek,et al.  The activities of amyloids from a structural perspective , 2016, Nature.

[326]  Sen Xin,et al.  Peptide Self-Assembled Biofilm with Unique Electron Transfer Flexibility for Highly Efficient Visible-Light-Driven Photocatalysis. , 2015, ACS nano.

[327]  D. Riesner,et al.  Aggregation and amyloid fibril formation of the prion protein is accelerated in the presence of glycogen. , 2008, Rejuvenation research.

[328]  Atanas V Koulov,et al.  Functional amyloid--from bacteria to humans. , 2007, Trends in biochemical sciences.

[329]  I. Hamley,et al.  Self-assembly of a peptide amphiphile: transition from nanotape fibrils to micelles , 2013 .

[330]  Rohit K. Sharma,et al.  Self-assembly of aromatic α-amino acids into amyloid inspired nano/micro scaled architects. , 2017, Materials science & engineering. C, Materials for biological applications.

[331]  J. Kovács,et al.  Reversible heat-induced dissociation of β2-microglobulin amyloid fibrils. , 2011, Biochemistry.

[332]  Michele Vendruscolo,et al.  Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments. , 2011, The Journal of chemical physics.

[333]  A. Matouschek Protein unfolding--an important process in vivo? , 2003, Current opinion in structural biology.

[334]  O. Inganäs,et al.  Protein Nanofibrils Balance Colours in Organic White‐Light‐Emitting Diodes , 2012 .

[335]  Alexander K. Buell,et al.  A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence , 2013, ChemBioChem.

[336]  I D Campbell,et al.  Amyloid fibril formation by an SH3 domain. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[337]  S. W. Davies,et al.  Amyloid, prions, and other protein aggregates , 2000 .

[338]  A. Fink The Aggregation and Fibrillation of α-Synuclein , 2006 .

[339]  S. Sen,et al.  Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif* , 2016, The Journal of Biological Chemistry.

[340]  K. Dawson,et al.  Dual effect of amino modified polystyrene nanoparticles on amyloid β protein fibrillation. , 2010, ACS chemical neuroscience.

[341]  Ericka Stricklin-Parker,et al.  Ann , 2005 .

[342]  Peter Schuck,et al.  Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. , 2002, Biophysical journal.

[343]  R. Mezzenga,et al.  New biocompatible thermo-reversible hydrogels from PNiPAM-decorated amyloid fibrils. , 2011, Chemical communications.

[344]  P. Faller,et al.  Amyloid fibrils: modulation of formation and structure by copper(II) , 2008 .

[345]  C. Roux,et al.  Polymorphism and higher order structures of protein nanofibers from crude mixtures of fish lens crystallins: toward useful materials. , 2012, Biopolymers.

[346]  C. Dobson,et al.  Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution , 2003, Journal of Molecular Medicine.

[347]  Rustam Azimov,et al.  The channel hypothesis of Alzheimer’s disease: current status , 2002, Peptides.

[348]  Qianli Zou,et al.  Peptide‐Modulated Self‐Assembly of Chromophores toward Biomimetic Light‐Harvesting Nanoarchitectonics , 2016, Advanced materials.

[349]  N. Greenfield Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions , 2006, Nature Protocols.

[350]  M. Mahmoudi,et al.  Graphene oxide strongly inhibits amyloid beta fibrillation. , 2012, Nanoscale.

[351]  Jozef Adamcik,et al.  Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons. , 2016, Angewandte Chemie.

[352]  Jonathan S. Weissman,et al.  The physical basis of how prion conformations determine strain phenotypes , 2006, Nature.

[353]  G. Nienhaus,et al.  Motif‐Designed Peptide Nanofibers Decorated with Graphene Quantum Dots for Simultaneous Targeting and Imaging of Tumor Cells , 2015 .

[354]  H. Scheraga,et al.  Experimental and theoretical aspects of protein folding. , 1975, Advances in protein chemistry.

[355]  Toshinori Sato,et al.  Density of GM1 in nanoclusters is a critical factor in the formation of a spherical assembly of amyloid β-protein on synaptic plasma membranes. , 2013, Langmuir : the ACS journal of surfaces and colloids.

[356]  S. Dewhurst,et al.  Oligovalent amyloid-binding agents reduce SEVI-mediated enhancement of HIV-1 infection. , 2012, Journal of the American Chemical Society.

[357]  R. Apkarian,et al.  Imaging amyloid β peptide oligomeric particles in solution , 2005 .

[358]  L. Adler-Abramovich,et al.  Extension of the generic amyloid hypothesis to nonproteinaceous metabolite assemblies , 2015, Science Advances.

[359]  Jennifer C. Lee,et al.  Amyloid Triangles, Squares, and Loops of Apolipoprotein C-III , 2014, Biochemistry.

[360]  R. Parker,et al.  The Nonequilibrium Phase and Glass Transition Behavior of β-Lactoglobulin , 2005 .

[361]  Haifeng Dong,et al.  Graphene quantum dots for the inhibition of β amyloid aggregation. , 2015, Nanoscale.

[362]  G. Howlett,et al.  Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I , 2010, Proceedings of the National Academy of Sciences.

[363]  G. McRae,et al.  A three-stage kinetic model of amyloid fibrillation. , 2007, Biophysical journal.

[364]  Christopher J Roberts,et al.  Non‐native protein aggregation kinetics , 2007, Biotechnology and bioengineering.

[365]  I. Hamley,et al.  Hydrogelation and self-assembly of Fmoc-tripeptides: unexpected influence of sequence on self-assembled fibril structure, and hydrogel modulus and anisotropy. , 2010, Langmuir : the ACS journal of surfaces and colloids.

[366]  R. Zhou,et al.  Destruction of amyloid fibrils by graphene through penetration and extraction of peptides. , 2015, Nanoscale.

[367]  C. Roberts,et al.  Controlling the Physical Dimensions of Peptide Nanotubes by Supramolecular Polymer Coassembly. , 2016, ACS nano.

[368]  F. Hartl,et al.  Principles of protein folding in the cellular environment. , 1999, Current opinion in structural biology.

[369]  M. Leone,et al.  Secondary nucleation and accessible surface in insulin amyloid fibril formation. , 2008, The journal of physical chemistry. B.

[370]  R. Liskamp,et al.  pH-controlled aggregation polymorphism of amyloidogenic Aβ(16-22): insights for obtaining peptide tapes and peptide nanotubes, as function of the N-terminal capping moiety. , 2014, European journal of medicinal chemistry.

[371]  Walraj S. Gosal,et al.  Fibrillar beta-lactoglobulin gels: Part 2. Dynamic mechanical characterization of heat-set systems. , 2004, Biomacromolecules.

[372]  R. Kayed,et al.  Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain*♦ , 2011, The Journal of Biological Chemistry.

[373]  P. Fraser,et al.  Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth. , 1999, European journal of biochemistry.

[374]  Jennifer C. Lee,et al.  Membrane remodeling by α-synuclein and effects on amyloid formation. , 2013, Journal of the American Chemical Society.

[375]  T. Chikuma,et al.  Dependence pH and proposed mechanism for aggregation of Alzheimer's disease-related amyloid-β(1-42) protein , 2015 .

[376]  Gang Wei,et al.  Self-assembled peptide nanofibers on graphene oxide as a novel nanohybrid for biomimetic mineralization of hydroxyapatite , 2015 .

[377]  A. Caflisch,et al.  Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria. , 2012, Nature chemical biology.

[378]  Jin-Mi Jung,et al.  Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate. , 2008, Biomacromolecules.

[379]  Driss El Moustaine,et al.  Full‐length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways , 2008, The FEBS journal.

[380]  M. Morbidelli,et al.  Contribution of Electrostatics in the Fibril Stability of a Model Ionic-Complementary Peptide. , 2015, Biomacromolecules.

[381]  M. Cotte,et al.  Microspectroscopy (μFTIR) reveals co-localization of lipid oxidation and amyloid plaques in human Alzheimer disease brains. , 2014, Analytical chemistry.

[382]  J. Enghild,et al.  Widespread Abundance of Functional Bacterial Amyloid in Mycolata and Other Gram-Positive Bacteria , 2009, Applied and Environmental Microbiology.

[383]  E. M. Jones,et al.  Structure-based design of functional amyloid materials. , 2014, Journal of the American Chemical Society.

[384]  M. Baigorí,et al.  Towards efficient biocatalysts: photo-immobilization of a lipase on novel lysozyme amyloid-like nanofibrils , 2016 .

[385]  V. Uversky,et al.  Why are “natively unfolded” proteins unstructured under physiologic conditions? , 2000, Proteins.

[386]  H. Risselada,et al.  Gold‐Induced Fibril Growth: The Mechanism of Surface‐Facilitated Amyloid Aggregation , 2016, Angewandte Chemie.

[387]  G. G. Stokes "J." , 1890, The New Yale Book of Quotations.

[388]  R. Mezzenga,et al.  Hybrid Amyloid Membranes for Continuous Flow Catalysis. , 2015, Langmuir : the ACS journal of surfaces and colloids.

[389]  V. Martorana,et al.  Amyloid gels: precocious appearance of elastic properties during the formation of an insulin fibrillar network. , 2010, Langmuir : the ACS journal of surfaces and colloids.

[390]  V. Martorana,et al.  Thermodynamic versus conformational metastability in fibril-forming lysozyme solutions. , 2012, The journal of physical chemistry. B.

[391]  I. Hamley The amyloid beta peptide: a chemist's perspective. Role in Alzheimer's and fibrillization. , 2012, Chemical reviews.

[392]  Ian W. Hamley,et al.  Self-assembly of amphiphilic peptides , 2011 .

[393]  Michele Vendruscolo,et al.  Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation , 2016, Nature Communications.

[394]  K. Matsuzaki,et al.  Formation of toxic Abeta(1-40) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: polymorphisms in Abeta(1-40) fibrils. , 2008, Journal of molecular biology.

[395]  O. Inganäs,et al.  Electrochemical devices made from conducting nanowire networks self-assembled from amyloid fibrils and alkoxysulfonate PEDOT. , 2008, Nano letters.

[396]  A. Miranker,et al.  Recent Insight in Islet Amyloid Polypeptide Morphology, Structure, Membrane Interaction, and Toxicity in Type 2 Diabetes , 2015, Journal of diabetes research.

[397]  K. Kar,et al.  Capsaicin-Coated Silver Nanoparticles Inhibit Amyloid Fibril Formation of Serum Albumin. , 2016, Biochemistry.

[398]  A. Casini,et al.  Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of amyloid-beta1-42: an AFM study. , 2010, Journal of Alzheimer's disease : JAD.

[399]  K. Ono,et al.  Anti-amyloidogenic therapies: strategies for prevention and treatment of Alzheimer’s disease , 2006, Cellular and Molecular Life Sciences CMLS.

[400]  R. Mezzenga,et al.  Amyloid Directed Synthesis of Titanium Dioxide Nanowires and Their Applications in Hybrid Photovoltaic Devices , 2012 .

[401]  C. Dobson,et al.  Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. , 2015, Nature chemical biology.

[402]  Xuehai Yan,et al.  Self-assembly and application of diphenylalanine-based nanostructures. , 2010, Chemical Society reviews.

[403]  A. Rich,et al.  Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[404]  David J Hayne,et al.  Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease. , 2014, Chemical Society reviews.

[405]  Tuomas P. J. Knowles,et al.  On the lag phase in amyloid fibril formation , 2015, Physical chemistry chemical physics : PCCP.

[406]  Michele Vendruscolo,et al.  Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism , 2013, Proceedings of the National Academy of Sciences.

[407]  R. Sauer,et al.  Stability and DNA Binding of the Phd Protein of the Phage P1 Plasmid Addiction System* , 1999, The Journal of Biological Chemistry.

[408]  R. Mezzenga,et al.  Bridging the gap between the nanostructural organization and macroscopic interfacial rheology of amyloid fibrils at liquid interfaces. , 2014, Langmuir : the ACS journal of surfaces and colloids.

[409]  Sara Linse,et al.  Quantification of the concentration of Aβ42 propagons during the lag phase by an amyloid chain reaction assay. , 2014, Journal of the American Chemical Society.

[410]  Alexander K. Buell,et al.  Protein microgels from amyloid fibril networks. , 2015, ACS nano.

[411]  R. Garifullin,et al.  Amyloid-like peptide nanofiber templated titania nanostructures as dye sensitized solar cell anodic materials , 2013 .

[412]  V. Uversky,et al.  Partially folded intermediates in insulin fibrillation. , 2003, Biochemistry.

[413]  R. Mezzenga,et al.  The interplay between carbon nanomaterials and amyloid fibrils in bio-nanotechnology. , 2013, Nanoscale.

[414]  S. Hoffmann,et al.  Mechanical stress affects glucagon fibrillation kinetics and fibril structure. , 2011, Langmuir : the ACS journal of surfaces and colloids.

[415]  M. Morbidelli,et al.  Time evolution of amyloid fibril length distribution described by a population balance model , 2012 .

[416]  Honggang Cui,et al.  Supramolecular nanostructures formed by anticancer drug assembly. , 2013, Journal of the American Chemical Society.

[417]  Richard D. Leapman,et al.  Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils , 2005, Science.

[418]  J. Samitier,et al.  Modulation of Aβ42 fìbrillogenesis by glycosaminoglycan structure , 2010, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[419]  A. Gräslund,et al.  The Aβ peptide forms non-amyloid fibrils in the presence of carbon nanotubes. , 2014, Nanoscale.

[420]  G. Belfort,et al.  Surface-enhanced nucleation of insulin amyloid fibrillation. , 2008, Biochemical and biophysical research communications.

[421]  H. Cui,et al.  One-step fabrication of self-assembled peptide thin films with highly dispersed noble metal nanoparticles. , 2013, Langmuir : the ACS journal of surfaces and colloids.

[422]  R. Mezzenga,et al.  Magnetic-responsive hybrids of Fe3O4 nanoparticles with β-lactoglobulin amyloid fibrils and nanoclusters. , 2013, ACS nano.

[423]  Costas Fotakis,et al.  Directed three-dimensional patterning of self-assembled peptide fibrils. , 2008, Nano letters.

[424]  R. Yoshida Design of Functional Polymer Gels and Their Application to Biomimetic Materials , 2005 .

[425]  F. Ferrone,et al.  Analysis of protein aggregation kinetics. , 1999, Methods in enzymology.

[426]  R. Mezzenga,et al.  Study of amyloid fibrils via atomic force microscopy , 2012 .

[427]  C. Dobson,et al.  The amyloid state and its association with protein misfolding diseases , 2014, Nature Reviews Molecular Cell Biology.

[428]  J. Fantini,et al.  Controlled aggregation of adenine by sugars: physicochemical studies, molecular modelling simulations of sugar-aromatic CH-pi stacking interactions, and biological significance. , 2008, Physical chemistry chemical physics : PCCP.

[429]  M. Michikawa Cholesterol paradox: Is high total or low HDL cholesterol level a risk for Alzheimer's disease? , 2003, Journal of neuroscience research.

[430]  R. Tycko,et al.  Molecular structures of amyloid and prion fibrils: consensus versus controversy. , 2013, Accounts of chemical research.

[431]  M. Michikawa The role of cholesterol in pathogenesis of Alzheimer's disease: dual metabolic interaction between amyloid beta-protein and cholesterol. , 2003, Molecular neurobiology.

[432]  Jae Hong Kim,et al.  Beta-Sheet-Forming, Self-Assembled Peptide Nanomaterials towards Optical, Energy, and Healthcare Applications. , 2015, Small.

[433]  Mun'delanji C. Vestergaard,et al.  Selective localization of Alzheimer's amyloid beta in membrane lateral compartments , 2012 .

[434]  Sang Won Suh,et al.  Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains , 2000, Brain Research.

[435]  Andrew M. Smith,et al.  Designing peptide based nanomaterials. , 2008, Chemical Society reviews.

[436]  Nathan J. Cobb,et al.  Prion Protein Amyloid Formation under Native-like Conditions Involves Refolding of the C-terminal α-Helical Domain* , 2008, Journal of Biological Chemistry.

[437]  J. Lu,et al.  Solvent Controlled Structural Transition of KI4K Self-Assemblies: from Nanotubes to Nanofibrils. , 2015, Langmuir : the ACS journal of surfaces and colloids.

[438]  M. Tena-Solsona,et al.  Tetrapeptidic molecular hydrogels: self-assembly and co-aggregation with amyloid fragment Aβ1-40. , 2014, Chemistry.

[439]  Robert C. Lee,et al.  Self-assembly of amelogenin proteins at the water-oil interface. , 2011, European journal of oral sciences.

[440]  Michele Vendruscolo,et al.  Direct Observation of the Three Regions in α-Synuclein that Determine its Membrane-Bound Behaviour , 2014, Nature Communications.

[441]  Gang Wei,et al.  Alternate layer-by-layer assembly of graphene oxide nanosheets and fibrinogen nanofibers on a silicon substrate for a biomimetic three-dimensional hydroxyapatite scaffold. , 2014, Journal of materials chemistry. B.

[442]  C. Glabe,et al.  Structural Classification of Toxic Amyloid Oligomers* , 2008, Journal of Biological Chemistry.

[443]  Julian C. W. Willis,et al.  The length distribution of frangible biofilaments. , 2015, The Journal of chemical physics.

[444]  S. Ventura,et al.  Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals , 2016, PLoS pathogens.

[445]  K. Karatzas,et al.  Hybrid membrane biomaterials from self-assembly in polysaccharide and peptide amphiphile mixtures: controllable structural and mechanical properties and antimicrobial activity , 2017 .

[446]  Dhiman Ghosh,et al.  Implantable amyloid hydrogels for promoting stem cell differentiation to neurons , 2016 .

[447]  Daan Frenkel,et al.  Crucial role of nonspecific interactions in amyloid nucleation , 2014, Proceedings of the National Academy of Sciences.

[448]  Anne-Kathrin Born,et al.  Amyloid‐Hydroxyapatite Bone Biomimetic Composites , 2014, Advanced materials.

[449]  Scott J. Hultgren,et al.  Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation , 2002, Science.

[450]  C. Sachse,et al.  Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils , 2007, Proceedings of the National Academy of Sciences.

[451]  Chan Beum Park,et al.  Insulin amyloid fibrillation at above 100°C: New insights into protein folding under extreme temperatures , 2004 .

[452]  V. Uversky Natively unfolded proteins: A point where biology waits for physics , 2002, Protein science : a publication of the Protein Society.

[453]  Michele Vendruscolo,et al.  From macroscopic measurements to microscopic mechanisms of protein aggregation. , 2012, Journal of molecular biology.

[454]  Alexander K. Buell,et al.  Population of nonnative states of lysozyme variants drives amyloid fibril formation. , 2011, Journal of the American Chemical Society.

[455]  Tracy O'Connor,et al.  Protein aggregation diseases: pathogenicity and therapeutic perspectives , 2010, Nature Reviews Drug Discovery.

[456]  A. Dexter Interfacial and emulsifying properties of designed β-strand peptides. , 2010, Langmuir : the ACS journal of surfaces and colloids.

[457]  Lucio Isa,et al.  Non-equilibrium nature of two-dimensional isotropic and nematic coexistence in amyloid fibrils at liquid interfaces , 2013, Nature Communications.

[458]  Michele Vendruscolo,et al.  Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation , 2014, Proceedings of the National Academy of Sciences.

[459]  B. Abel,et al.  Structure‐Making Effects of Metal Nanoparticles in Amyloid Peptide Fibrillation , 2015 .

[460]  I. Hamley,et al.  Bioactive films produced from self-assembling peptide amphiphiles as versatile substrates for tuning cell adhesion and tissue architecture in serum-free conditions. , 2013, Journal of materials chemistry. B.

[461]  R. Mezzenga,et al.  Functionalization of multiwalled carbon nanotubes and their pH-responsive hydrogels with amyloid fibrils. , 2012, Langmuir : the ACS journal of surfaces and colloids.

[462]  D. Eisenberg,et al.  Toxic fibrillar oligomers of amyloid-β have cross-β structure , 2012, Proceedings of the National Academy of Sciences.

[463]  Jan C. M. van Hest,et al.  Peptide- and Protein-Based Hydrogels , 2012 .

[464]  K. Dawson,et al.  Inhibition of IAPP and IAPP(20-29) fibrillation by polymeric nanoparticles. , 2010, Langmuir : the ACS journal of surfaces and colloids.

[465]  Robert Forchheimer,et al.  Electrochromic Electrochemical Transistors Gated With Polyelectrolyte-Decorated Amyloid Fibrils , 2013, Journal of Display Technology.

[466]  A. Stensballe,et al.  Major proteomic changes associated with amyloid-induced biofilm formation in Pseudomonas aeruginosa PAO1. , 2015, Journal of proteome research.

[467]  C. Dobson,et al.  A Partially Structured Species of β2-Microglobulin Is Significantly Populated under Physiological Conditions and Involved in Fibrillogenesis* , 2001, The Journal of Biological Chemistry.

[468]  J. V. Hest,et al.  Stimulus responsive peptide based materials. , 2010, Chemical Society reviews.

[469]  J. Vörös,et al.  Engineering the Extracellular Environment: Strategies for Building 2D and 3D Cellular Structures , 2010, Advanced materials.

[470]  J. Hofrichter,et al.  Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. , 1985, Journal of molecular biology.

[471]  Judianne Davis,et al.  Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils , 2010, Nature Structural &Molecular Biology.

[472]  S. Radford,et al.  Fibril Fragmentation Enhances Amyloid Cytotoxicity*♦ , 2009, The Journal of Biological Chemistry.