Surface-catalyzed amyloid fibril formation.
TLDR
In the present investigation, the in vitro assembly of a recombinant amyloidogenic light chain variable domain, SMA, on various surfaces was monitored using atomic force microscopy and the mechanism of fibril formation on the surfaces was significantly different from in solution.About:
This article is published in Journal of Biological Chemistry.The article was published on 2002-12-27 and is currently open access. It has received 245 citations till now. The article focuses on the topics: Fibril.read more
Citations
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Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences*
TL;DR: Theoretical and experimental approaches to the characterization of crowding- and confinement-induced effects in systems approaching the complexity of living organisms are suggested.
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Membrane and surface interactions of Alzheimer's Aβ peptide--insights into the mechanism of cytotoxicity.
TL;DR: Oligomeric Aβ has been observed to bind more avidly to membranes and cause greater permeation than fibrillar Aβ, which has implications with respect to understanding the causes of Alzheimer’s disease.
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Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins.
TL;DR: A review of investigations of the interactions of amyloidogenic polypeptides and their aggregated states with membranes highlights the significant role played by fluorescence techniques in unraveling the nature ofAmyloid fibrils and their interactions and effects on membranes.
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Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
TL;DR: The authors showed that membranes containing phosphatidylserine (PS), a negatively charged phospholipid, induce a rapid formation of fibers by a variety of proteins, viz., lysozyme, insulin, glyceraldehyde-3-phosphate dehydrogenase, myoglobin, transthyretin, cytochrome c, histone H1, and α-lactalbumin.
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The role of lipid-protein interactions in amyloid-type protein fibril formation.
TL;DR: The present review summarizes the principal factors responsible for the enhancement of fibril formation in a membrane environment, viz. structural transformation of polypeptide chain into a partially folded conformation, increase of the local concentration of a protein upon its membrane binding, and aggregation-favoring orientation of the bound protein.
References
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Diffusible, nonfibrillar ligands derived from Aβ1–42 are potent central nervous system neurotoxins
Mary P. Lambert,A. K. Barlow,Brett A. Chromy,C. Edwards,R. Freed,M. Liosatos,Todd E. Morgan,Irina Rozovsky,Barbara L. Trommer,Kirsten L. Viola,Pat Wals,Chuan Zhang,Caleb E. Finch,Grant A. Krafft,William L. Klein +14 more
TL;DR: It is hypothesized that impaired synaptic plasticity and associated memory dysfunction during early stage Alzheimer's disease and severe cellular degeneration and dementia during end stage could be caused by the biphasic impact of Abeta-derived diffusible ligands acting upon particular neural signal transduction pathways.
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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.
TL;DR: Thioflavine T associates rapidly with aggregated fibrils of the synthetic β/A4‐derived peptides β( 1–28) and β(1–40), giving rise to a new excitation maximum at 450 nm and enhanced emission at 482 nm, as opposed to the 385 nm and 445 nm of the free dye.
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Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism
Liza Nielsen,Ritu Khurana,Alisa C. Coats,Sven Frokjaer,Jens Brange,Sandip Vyas,Vladimir N. Uversky,Anthony L. Fink +7 more
TL;DR: The results indicated that both nucleation and fibril growth were controlled by hydrophobic and electrostatic interactions.
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Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease†
Michael J. Volles,Seung-Jae Lee,Jean-Christophe Rochet,Mark D. Shtilerman,Tomas T. Ding,Jeffrey C. Kessler,Peter T. Lansbury +6 more
TL;DR: It is reported here that protofibrils differ markedly from fibrils with respect to their interactions with synthetic membranes, and the possibility that the toxicity of alpha-synuclein fibrillization may derive from an oligomeric intermediate, rather than the fibril, has implications regarding the design of therapeutics for PD.
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Amyloid diseases: abnormal protein aggregation in neurodegeneration.
TL;DR: This review will focus on biophysical studies of protein aggregation in AD and FAP, where mechanistic models connecting pathological and genetic data to clinical disease are beginning to emerge.