Early Kinetics of Amyloid Fibril Formation Reveals Conformational Reorganisation of Initial Aggregates

2007 ◽  
Vol 366 (4) ◽  
pp. 1351-1363 ◽  
Author(s):  
N. Cerdà-Costa ◽  
A. Esteras-Chopo ◽  
F.X. Avilés ◽  
L. Serrano ◽  
V. Villegas
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Kinetics Of

scholarly journals Effect of Association State and Conformational Stability on the Kinetics of Immunoglobulin Light Chain Amyloid Fibril Formation at Physiological pH

2002 ◽  
Vol 277 (15) ◽  
pp. 12657-12665 ◽  
Author(s):  
Pierre O. Souillac ◽  
Vladimir N. Uversky ◽  
Ian S. Millett ◽  
Ritu Khurana ◽  
Sebastian Doniach ◽  
...  
Keyword(s):  
Light Chain ◽  
Amyloid Fibril ◽  
Conformational Stability ◽  
Fibril Formation ◽  
Immunoglobulin Light Chain ◽  
Amyloid Fibril Formation ◽  
Kinetics Of ◽  
Association State

Elucidating the Kinetics of β-Amyloid Fibril Formation

2005 ◽  
pp. 106-118 ◽  
Author(s):  
Nadia J. Edwin ◽  
Grigor B. Bantchev ◽  
Paul S. Russo ◽  
Robert P. Hammer ◽  
Robin L. McCarley
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Kinetics Of

scholarly journals Inhibition of Protein Aggregation by Several Antioxidants

2018 ◽  
Vol 2018 ◽  
pp. 1-12 ◽  
Author(s):  
Samra Hasanbašić ◽  
Alma Jahić ◽  
Selma Berbić ◽  
Magda Tušek Žnidarič ◽  
Eva Žerovnik
Keyword(s):  
Vitamin C ◽  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Tht Fluorescence ◽  
Shared Property ◽  
High Concentrations ◽  
Kinetics Of

Amyloid fibril formation is a shared property of all proteins; therefore, model proteins can be used to study this process. We measured protein aggregation of the model amyloid-forming protein stefin B in the presence and absence of several antioxidants. Amyloid fibril formation by stefin B was routinely induced at pH 5 and 10% TFE, at room temperature. The effects of antioxidants NAC, vitamin C, vitamin E, and the three polyphenols resveratrol, quercetin, and curcumin on the kinetics of fibril formation were followed using ThT fluorescence. Concomitantly, the morphology and amount of the aggregates and fibrils were checked by transmission electron microscopy (TEM). The concentration of the antioxidants was varied, and it was observed that different modes of action apply at low or high concentrations relative to the binding constant. In order to obtain more insight into the possible mode of binding, docking of NAC, vitamin C, and all three polyphenols was done to the monomeric form of stefin B.

scholarly journals Network Hamiltonian models reveal pathways to amyloid fibril formation

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Yue Yu ◽  
Gianmarc Grazioli ◽  
Megha H. Unhelkar ◽  
Rachel W. Martin ◽  
Carter T. Butts
Keyword(s):  
Amyloid Fibril ◽  
Prion Diseases ◽  
Data Bank ◽  
Fibril Formation ◽  
Toxic Species ◽  
Hamiltonian Models ◽  
Amyloid Fibril Formation ◽  
Wide Range ◽  
Kinetics Of

Abstract Amyloid fibril formation is central to the etiology of a wide range of serious human diseases, such as Alzheimer’s disease and prion diseases. Despite an ever growing collection of amyloid fibril structures found in the Protein Data Bank (PDB) and numerous clinical trials, therapeutic strategies remain elusive. One contributing factor to the lack of progress on this challenging problem is incomplete understanding of the mechanisms by which these locally ordered protein aggregates self-assemble in solution. Many current models of amyloid deposition diseases posit that the most toxic species are oligomers that form either along the pathway to forming fibrils or in competition with their formation, making it even more critical to understand the kinetics of fibrillization. A recently introduced topological model for aggregation based on network Hamiltonians is capable of recapitulating the entire process of amyloid fibril formation, beginning with thousands of free monomers and ending with kinetically accessible and thermodynamically stable amyloid fibril structures. The model can be parameterized to match the five topological classes encompassing all amyloid fibril structures so far discovered in the PDB. This paper introduces a set of network statistical and topological metrics for quantitative analysis and characterization of the fibrillization mechanisms predicted by the network Hamiltonian model. The results not only provide insight into different mechanisms leading to similar fibril structures, but also offer targets for future experimental exploration into the mechanisms by which fibrils form.

scholarly journals Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e7554
Author(s):  
Mantas Ziaunys ◽  
Tomas Sneideris ◽  
Vytautas Smirnovas
Keyword(s):  
Neurodegenerative Disorders ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Formation ◽  
Amyloid Aggregation ◽  
Deep Blue ◽  
Amyloid Fibril Formation ◽  
Kinetics Of ◽  
Kinetics Of Fibril Formation

Protein aggregation into amyloid fibrils has been linked to multiple neurodegenerative disorders. Determining the kinetics of fibril formation, as well as their structural stability are important for the mechanistic understanding of amyloid aggregation. Tracking both fibril association and dissociation is usually performed by measuring light scattering of the solution or fluorescence of amyloid specific dyes, such as thioflavin-T. A possible addition to these methods is the recently discovered deep-blue autofluorescence (dbAF), which is linked to amyloid formation. In this work we explore the potential of this phenomenon to monitor amyloid fibril formation and dissociation, as well as show its possible relation to fibril size rather than amyloid structure.

scholarly journals A Generic Crystallization-like Model That Describes the Kinetics of Amyloid Fibril Formation

2012 ◽  
Vol 287 (36) ◽  
pp. 30585-30594 ◽  
Author(s):  
Rosa Crespo ◽  
Fernando A. Rocha ◽  
Ana M. Damas ◽  
Pedro M. Martins
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Kinetics Of

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

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