Tryptophan-galactosylamine conjugates inhibit and disaggregate amyloid fibrils of Aβ42 and hIAPP peptides while reducing their toxicity

[1]  E. Gazit,et al.  Tryptophan-glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations. , 2019, Chemical communications.

[2]  E. Gazit,et al.  Naphthoquinone Tryptophan Hybrids: A Promising Small Molecule Scaffold for Mitigating Aggregation of Amyloidogenic Proteins and Peptides , 2019, Front. Cell Dev. Biol..

[3]  E. Gazit,et al.  Antagonistic Activity of Naphthoquinone-Based Hybrids toward Amyloids Associated with Alzheimer's Disease and Type-2 Diabetes. , 2019, ACS chemical neuroscience.

[4]  Zhaoqian Su,et al.  Thermodynamic Stability of Polar and Nonpolar Amyloid Fibrils. , 2019, Journal of chemical theory and computation.

[5]  C. Dobson,et al.  Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates , 2019, Science Advances.

[6]  E. Gazit,et al.  Novel Mannitol-Based Small Molecules for Inhibiting Aggregation of α-Synuclein Amyloids in Parkinson's Disease , 2019, Front. Mol. Biosci..

[7]  R. Ramos,et al.  Epidemiology of dementia: prevalence and incidence estimates using validated electronic health records from primary care , 2019, Clinical epidemiology.

[8]  E. Gazit,et al.  Novel model of secreted human tau protein reveals the impact of the abnormal N-glycosylation of tau on its aggregation propensity , 2019, Scientific Reports.

[9]  A. Bobylev,et al.  Congo Red and amyloids: history and relationship , 2018, Bioscience reports.

[10]  A. Sabri,et al.  Hyperglycemia-Driven Neuroinflammation Compromises BBB Leading to Memory Loss in Both Diabetes Mellitus (DM) Type 1 and Type 2 Mouse Models , 2018, Molecular Neurobiology.

[11]  P. Manzanares,et al.  Tryptophan-Containing Dual Neuroprotective Peptides: Prolyl Endopeptidase Inhibition and Caenorhabditis elegans Protection from β-Amyloid Peptide Toxicity , 2018, International journal of molecular sciences.

[12]  Wen Zhou,et al.  Application of Mono‐ and Disaccharides in Drug Targeting and Efficacy , 2018, ChemMedChem.

[13]  N. Phillips,et al.  Etiology of type 2 diabetes and Alzheimer's disease: Exploring the mitochondria. , 2018, Mitochondrion.

[14]  T. Sandahl,et al.  The Galactose Elimination Capacity test may monitor treatment response and disease progression in patients with Wilson Disease , 2018 .

[15]  E. Chatani,et al.  Recent progress on understanding the mechanisms of amyloid nucleation , 2018, Biophysical Reviews.

[16]  Z. Arvanitakis,et al.  Review: Relationship of type 2 diabetes to human brain pathology , 2018, Neuropathology and applied neurobiology.

[17]  A. Ghosh,et al.  A Peptide Based Pro-drug Disrupts Alzheimer’s Amyloid into Non-toxic Species and Reduces Aβ Induced Toxicity In Vitro , 2018, International Journal of Peptide Research and Therapeutics.

[18]  H. Fuchs,et al.  Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice , 2018, Scientific Reports.

[19]  E. Gazit,et al.  Mechanistic insights into remodeled Tau-derived PHF6 peptide fibrils by Naphthoquinone-Tryptophan hybrids , 2018, Scientific Reports.

[20]  Bhupinder Singh,et al.  Recent advances in galactose-engineered nanocarriers for the site-specific delivery of siRNA and anticancer drugs. , 2017, Drug discovery today.

[21]  C. Soto,et al.  Induction of IAPP amyloid deposition and associated diabetic abnormalities by a prion-like mechanism , 2017, The Journal of experimental medicine.

[22]  S. Radford,et al.  Small molecule probes of protein aggregation. , 2017, Current opinion in chemical biology.

[23]  E. Gazit,et al.  Inhibition of the Aggregation and Toxicity of the Minimal Amyloidogenic Fragment of Tau by Its Pro-Substituted Analogues. , 2017, Chemistry.

[24]  P. Král,et al.  Formation of Apoptosis‐Inducing Amyloid Fibrils by Tryptophan , 2017 .

[25]  Vojtěch Spiwok,et al.  CH/π Interactions in Carbohydrate Recognition , 2017, Molecules.

[26]  E. Gazit,et al.  Inhibition of amyloid oligomerization into different supramolecular architectures by small molecules: mechanistic insights and design rules. , 2017, Future medicinal chemistry.

[27]  Eugenia Trushina,et al.  Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease , 2017, Journal of Alzheimer's disease : JAD.

[28]  L. V. van Loon,et al.  Glucose Plus Fructose Ingestion for Post-Exercise Recovery—Greater than the Sum of Its Parts? , 2017, Nutrients.

[29]  L. Serpell,et al.  Amyloidogenicity and toxicity of the reverse and scrambled variants of amyloid‐β 1‐42 , 2017, FEBS letters.

[30]  Ashim Paul,et al.  Disaggregation of Amylin Aggregate by Novel Conformationally Restricted Aminobenzoic Acid containing α/β and α/γ Hybrid Peptidomimetics , 2017, Scientific Reports.

[31]  Tuomas P. J. Knowles,et al.  Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease , 2016, Proceedings of the National Academy of Sciences.

[32]  W. Suen,et al.  Antibody-Based Drugs and Approaches Against Amyloid-β Species for Alzheimer’s Disease Immunotherapy , 2016, Drugs & Aging.

[33]  Min-Seon Kim,et al.  Hyperglycemia Reduces Efficiency of Brain Networks in Subjects with Type 2 Diabetes , 2016, PloS one.

[34]  E. Gazit,et al.  Selective Inhibition of Aggregation and Toxicity of a Tau-Derived Peptide using Its Glycosylated Analogues. , 2016, Chemistry.

[35]  W. M. Hussein,et al.  Glycosylation, an effective synthetic strategy to improve the bioavailability of therapeutic peptides , 2016, Chemical science.

[36]  Q. Nguyen,et al.  Updates on the Clinical Trials in Diabetic Macular Edema , 2016, Middle East African journal of ophthalmology.

[37]  R. Mahalakshmi,et al.  Implications of aromatic–aromatic interactions: From protein structures to peptide models , 2015, Protein science : a publication of the Protein Society.

[38]  K. Kar,et al.  Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin , 2015, Amino Acids.

[39]  E. Zacco,et al.  Tailored Presentation of Carbohydrates on a Coiled Coil-Based Scaffold for Asialoglycoprotein Receptor Targeting. , 2015, ACS chemical biology.

[40]  Hans v Berlepsch,et al.  A Self-Assembling Peptide Scaffold for the Multivalent Presentation of Antigens. , 2015, Biomacromolecules.

[41]  D. Holtzman,et al.  Hyperglycemia modulates extracellular amyloid-β concentrations and neuronal activity in vivo. , 2015, The Journal of clinical investigation.

[42]  Ann Tiiman,et al.  In vitro fibrillization of Alzheimer’s amyloid-β peptide (1-42) , 2015 .

[43]  T. Bayer Proteinopathies, a core concept for understanding and ultimately treating degenerative disorders? , 2015, European Neuropsychopharmacology.

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

[45]  Ashim Paul,et al.  Inhibition of Alzheimer's amyloid-β peptide aggregation and its disruption by a conformationally restricted α/β hybrid peptide. , 2015, Chemical communications.

[46]  Shaoyi Jiang,et al.  Brazilin inhibits amyloid β-protein fibrillogenesis, remodels amyloid fibrils and reduces amyloid cytotoxicity , 2015, Scientific Reports.

[47]  M. Fändrich,et al.  Protein aggregation in Alzheimer’s disease: Aβ and τ and their potential roles in the pathogenesis of AD , 2015, Acta Neuropathologica.

[48]  Simone Lista,et al.  Advances in the therapy of Alzheimer’s disease: targeting amyloid beta and tau and perspectives for the future , 2015, Expert review of neurotherapeutics.

[49]  M. Barbagallo,et al.  Type 2 diabetes mellitus and Alzheimer's disease. , 2014, World journal of diabetes.

[50]  Hao Yu,et al.  Construction of efficacious hepatoma-targeted nanomicelles non-covalently functionalized with galactose for drug delivery , 2014 .

[51]  Shein-Chung Chow,et al.  Bioavailability and bioequivalence in drug development , 2014, Wiley interdisciplinary reviews. Computational statistics.

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

[53]  P. Chakrabarti,et al.  CH-π hydrogen bonds in biological macromolecules. , 2014, Physical chemistry chemical physics : PCCP.

[54]  Ashim Paul,et al.  Reversal of aggregation using β-breaker dipeptide containing peptides: Application to Aβ(1-40) self-assembly and its inhibition. , 2014, ACS chemical neuroscience.

[55]  C. Klein,et al.  Glycoengineering of Therapeutic Antibodies Enhances Monocyte/Macrophage-Mediated Phagocytosis and Cytotoxicity , 2014, The Journal of Immunology.

[56]  Joan-Emma Shea,et al.  Structural Similarities and Differences between Amyloidogenic and Non-Amyloidogenic Islet Amyloid Polypeptide (IAPP) Sequences and Implications for the Dual Physiological and Pathological Activities of These Peptides , 2013, PLoS Comput. Biol..

[57]  C. Pan,et al.  Galactose-based amphiphilic block copolymers: synthesis, micellization, and bioapplication. , 2013, Biomacromolecules.

[58]  J. Danielsson,et al.  Transient small molecule interactions kinetically modulate amyloid β peptide self‐assembly , 2012, FEBS letters.

[59]  N. M. Silva,et al.  Adjuvant and immunostimulatory effects of a D-galactose-binding lectin from Synadenium carinatum latex (ScLL) in the mouse model of vaccination against neosporosis , 2012, Veterinary Research.

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

[61]  Roni Scherzer-Attali,et al.  Generic inhibition of amyloidogenic proteins by two naphthoquinone–tryptophan hybrid molecules , 2012, Proteins.

[62]  Zeeshan Iqbal,et al.  The role of Galactose in human health and disease , 2012 .

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

[64]  A. Miranker,et al.  Concentration‐dependent transitions govern the subcellular localization of islet amyloid polypeptide , 2012, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[65]  B. Dahlbäck,et al.  Structural changes in apolipoproteins bound to nanoparticles. , 2011, Langmuir : the ACS journal of surfaces and colloids.

[66]  Fabio Biscarini,et al.  Kinetic characterization of amyloid-beta 1-42 aggregation with a multimethodological approach. , 2011, Analytical biochemistry.

[67]  Per Westermark,et al.  Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. , 2011, Physiological reviews.

[68]  D. Eisenberg,et al.  Macrocyclic β-Sheet Peptides That Inhibit the Aggregation of a Tau-Protein-Derived Hexapeptide , 2011, Journal of the American Chemical Society.

[69]  R. Kuroda,et al.  CD measurements of β-amyloid (1-40) and (1-42) in the condensed phase. , 2011, Biopolymers.

[70]  E. Gazit,et al.  Orally Administrated Cinnamon Extract Reduces β-Amyloid Oligomerization and Corrects Cognitive Impairment in Alzheimer's Disease Animal Models , 2011, PloS one.

[71]  J. Dordick,et al.  Aromatic Small Molecules Remodel Toxic Soluble Oligomers of Amyloid β through Three Independent Pathways* , 2010, The Journal of Biological Chemistry.

[72]  M. Stefani,et al.  Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity , 2010, The FEBS journal.

[73]  Amit Kumar,et al.  Inhibition of Aβ42 peptide aggregation by a binuclear ruthenium(II)-platinum(II) complex: Potential for multi-metal organometallics as anti-amyloid agents. , 2010, ACS chemical neuroscience.

[74]  Amedeo Caflisch,et al.  Complete Phenotypic Recovery of an Alzheimer's Disease Model by a Quinone-Tryptophan Hybrid Aggregation Inhibitor , 2010, PloS one.

[75]  T. Wolever The Glycaemic Index: A Physiological Classification of Dietary Carbohydrate , 2010 .

[76]  Bertrand Morel,et al.  The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry. , 2010, The journal of physical chemistry. B.

[77]  T. Zako,et al.  Amyloid oligomers: formation and toxicity of Aβ oligomers , 2010, The FEBS journal.

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

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

[80]  Colin L Masters,et al.  Aβ aggregation and possible implications in Alzheimer's disease pathogenesis , 2009, Journal of cellular and molecular medicine.

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

[82]  T. Wisniewski,et al.  Amyloid-β immunisation for Alzheimer's disease , 2008, The Lancet Neurology.

[83]  D. Walsh,et al.  Protein Aggregation in the Brain: The Molecular Basis for Alzheimer’s and Parkinson’s Diseases , 2008, Molecular medicine.

[84]  D. Ehrnhoefer,et al.  EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers , 2008, Nature Structural &Molecular Biology.

[85]  E. Carboni,et al.  Galactosylated dopamine enters into the brain, blocks the mesocorticolimbic system and modulates activity and scanning time in Naples high excitability rats , 2008, Neuroscience.

[86]  A. Jones,et al.  Physical basis of colors seen in Congo red-stained amyloid in polarized light , 2008, Laboratory Investigation.

[87]  P. Butler,et al.  Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. , 2008, Endocrine reviews.

[88]  Michele Vendruscolo,et al.  Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils , 2007, Science.

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

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

[91]  Amedeo Caflisch,et al.  Prediction of aggregation rate and aggregation‐prone segments in polypeptide sequences , 2005, Protein science : a publication of the Protein Society.

[92]  S. Chou,et al.  Inhibition of amyloid fibril formation of beta-amyloid peptides via the amphiphilic surfactants. , 2005, Biochimica et biophysica acta.

[93]  Michele Vendruscolo,et al.  Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. , 2005, Journal of molecular biology.

[94]  D. Raleigh,et al.  Role of aromatic interactions in amyloid formation by peptides derived from human Amylin. , 2004, Biochemistry.

[95]  Ehud Gazit,et al.  Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. , 2004, Biochemistry.

[96]  Per Westermark,et al.  Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes. , 2004, The Journal of clinical endocrinology and metabolism.

[97]  Christopher M Dobson,et al.  Principles of protein folding, misfolding and aggregation. , 2004, Seminars in cell & developmental biology.

[98]  P. Fraser,et al.  Identification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesis. , 2003, Journal of structural biology.

[99]  Ehud Gazit,et al.  A possible role for π‐stacking in the self‐assembly of amyloid fibrils , 2002, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[100]  J. Bernhagen,et al.  Amyloidogenicity of recombinant human pro-islet amyloid polypeptide (ProIAPP). , 2000, Chemistry & biology.

[101]  B. Ahrén,et al.  Islet amyloid and type 2 diabetes mellitus. , 2000, The New England journal of medicine.

[102]  A. Fernández-Mayoralas,et al.  Synthesis and biological studies of glycosyl dopamine derivatives as potential antiparkinsonian agents. , 2000, Carbohydrate research.

[103]  C. Betsholtz,et al.  Islet amyloid polypeptide (amylin)-deficient mice develop a more severe form of alloxan-induced diabetes. , 2000, American journal of physiology. Endocrinology and metabolism.

[104]  Lars Terenius,et al.  A Molecular Model of Alzheimer Amyloid β-Peptide Fibril Formation* , 1999, The Journal of Biological Chemistry.

[105]  K. Petry,et al.  The fundamental importance of human galactose metabolism: lessons from genetics and biochemistry. , 1998, Trends in genetics : TIG.

[106]  Florante A. Quiocho,et al.  Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units , 1987, Nature.

[107]  D. W. Hayden,et al.  Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[108]  Weilin Zhang,et al.  Targeting intrinsically disordered proteins at the edge of chaos. , 2019, Drug discovery today.

[109]  Pilar Ventosa-Andrés,et al.  DRUG SOLUBILITY : IMPORTANCE AND ENHANCEMENT TECHNIQUES , 2016 .

[110]  V. Taneja,et al.  Toxic species in amyloid disorders: Oligomers or mature fibrils , 2015, Annals of Indian Academy of Neurology.

[111]  S. Gras,et al.  Transmission electron microscopy of amyloid fibrils. , 2011, Methods in molecular biology.

[112]  Michèle Allard,et al.  Brain fuel metabolism, aging, and Alzheimer's disease. , 2011, Nutrition (Burbank, Los Angeles County, Calif.).

[113]  D. Selkoe Alzheimer's disease. , 2011, Cold Spring Harbor perspectives in biology.

[114]  N. Greenfield Using circular dichroism spectra to estimate protein secondary structure , 2007, Nature Protocols.

[115]  Kenneth H. Johnson,et al.  Staining methods for identification of amyloid in tissue. , 1999, Methods in enzymology.