A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence

Kinetic assay of seeded growth: The graph shows the variation in intrinsic fluorescence intensity of amyloid fibrils. Fluorescence increases during the seeded aggregation of α-synuclein seeds with α-synuclein monomeric protein (blue curve) but not when α-synuclein seeds are incubated with β-synuclein monomeric protein (black curve), thus showing that no seeded growth occurred in this case.

[1]  Shitong Li,et al.  Estrogen Rapidly Enhances Incisional Pain of Ovariectomized Rats Primarily through the G Protein-Coupled Estrogen Receptor , 2014, International journal of molecular sciences.

[2]  C. Dobson,et al.  Protein amyloids develop an intrinsic fluorescence signature during aggregation. , 2013, The Analyst.

[3]  Nicholas W. Smith,et al.  Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (aβ) self-assembly. , 2012, ACS chemical neuroscience.

[4]  Alexander K. Buell,et al.  A rationally designed six-residue swap generates comparability in the aggregation behavior of α-synuclein and β-synuclein. , 2012, Biochemistry.

[5]  Glyn L. Devlin,et al.  Metastability of native proteins and the phenomenon of amyloid formation. , 2011, Journal of the American Chemical Society.

[6]  Tuomas P. J. Knowles,et al.  Nucleated Polymerisation in the Presence of Pre-Formed Seed Filaments , 2011, International journal of molecular sciences.

[7]  Patrick Walsh,et al.  Solid-State NMR Characterization of Autofluorescent Fibrils Formed by the Elastin-Derived Peptide GVGVAGVG , 2011, Biomacromolecules.

[8]  Clemens F Kaminski,et al.  A FRET sensor for non-invasive imaging of amyloid formation in vivo. , 2011, Chemphyschem : a European journal of chemical physics and physical chemistry.

[9]  C. Kaminski,et al.  Design and application of a confocal microscope for spectrally resolved anisotropy imaging. , 2011, Optics express.

[10]  Alexander K. Buell,et al.  Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors. , 2010, Biophysical journal.

[11]  C. Dobson,et al.  ANS binding reveals common features of cytotoxic amyloid species. , 2010, ACS chemical biology.

[12]  O. Rolinski,et al.  Early detection of amyloid aggregation using intrinsic fluorescence. , 2010, Biosensors & bioelectronics.

[13]  Kyle L. Morris,et al.  The common architecture of cross-beta amyloid. , 2010, Journal of molecular biology.

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

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

[16]  C. Dobson,et al.  On the mechanism of nonspecific inhibitors of protein aggregation: dissecting the interactions of alpha-synuclein with Congo red and lacmoid. , 2009, Biochemistry.

[17]  Sara Linse,et al.  A facile method for expression and purification of the Alzheimer’s disease-associated amyloid β-peptide , 2009, The FEBS journal.

[18]  S. Radford,et al.  Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly , 2008, Proceedings of the National Academy of Sciences.

[19]  Roberto Cingolani,et al.  Charge transport and intrinsic fluorescence in amyloid-like fibrils , 2007, Proceedings of the National Academy of Sciences.

[20]  A. Jeyasekharan,et al.  A white light confocal microscope for spectrally resolved multidimensional imaging , 2007, Journal of microscopy.

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

[22]  Christopher M Dobson,et al.  Characterization of the nanoscale properties of individual amyloid fibrils , 2006, Proceedings of the National Academy of Sciences.

[23]  Mun'delanji C. Vestergaard,et al.  A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid beta aggregation. , 2005, Journal of the American Chemical Society.

[24]  V. Agrawal,et al.  A novel UV laser-induced visible blue radiation from protein crystals and aggregates: scattering artifacts or fluorescence transitions of peptide electrons delocalized through hydrogen bonding? , 2004, Archives of biochemistry and biophysics.

[25]  C. Dobson Protein folding and misfolding , 2003, Nature.

[26]  E. Mandelkow,et al.  Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments. , 2002, Biochemistry.

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

[28]  M. Citron,et al.  Parkinson's Disease-associated α-Synuclein Is More Fibrillogenic than β- and γ-Synuclein and Cannot Cross-seed Its Homologs* , 2000, The Journal of Biological Chemistry.

[29]  George B. Benedek,et al.  Kinetic theory of fibrillogenesis of amyloid β-protein , 1997 .

[30]  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.

[31]  C. Pennock,et al.  Interaction of water-soluble amyloid fibrils with Congo Red and thioflavine T. , 1969, Clinica chimica acta; international journal of clinical chemistry.

[32]  D. Teplow Preparation of amyloid β-protein for structural and functional studies , 2006 .