scholarly journals Kinetics of Fibril Formation by Polyalanine Peptides

2005 ◽  
Vol 280 (10) ◽  
pp. 9074-9082 ◽  
Author(s):  
Hung D. Nguyen ◽  
Carol K. Hall
Keyword(s):  
Fibril Formation ◽  
Kinetics Of ◽  
Kinetics Of Fibril Formation

Kinetics of Fibril Formation of Bovine κ-Casein Indicate a Conformational Rearrangement as a Critical Step in the Process

2008 ◽  
Vol 381 (5) ◽  
pp. 1267-1280 ◽  
Author(s):  
Joelle Leonil ◽  
Gwenaele Henry ◽  
Dianne Jouanneau ◽  
Marie-Madeleine Delage ◽  
Vincent Forge ◽  
...  
Keyword(s):  
Fibril Formation ◽  
Conformational Rearrangement ◽  
Critical Step ◽  
Kinetics Of ◽  
Kinetics Of Fibril Formation

scholarly journals Mouse Prion Protein Polymorphism Phe-108/Val-189 Affects the Kinetics of Fibril Formation and the Response to Seeding

2013 ◽  
Vol 288 (7) ◽  
pp. 4772-4781 ◽  
Author(s):  
Leonardo M. Cortez ◽  
Jitendra Kumar ◽  
Ludovic Renault ◽  
Howard S. Young ◽  
Valerie L. Sim
Keyword(s):  
Prion Protein ◽  
Fibril Formation ◽  
Protein Polymorphism ◽  
Kinetics Of ◽  
Kinetics Of Fibril Formation

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 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

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

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.

Kinetics of protein fibril formation: Methods and mechanisms

2017 ◽  
Vol 100 ◽  
pp. 3-10 ◽  
Author(s):  
E. Kiran Kumar ◽  
Neshatul Haque ◽  
N. Prakash Prabhu
Keyword(s):  
Fibril Formation ◽  
Protein Fibril ◽  
Kinetics Of

Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation:  Elucidation of the Molecular Mechanism†

Biochemistry ◽  
2001 ◽  
Vol 40 (20) ◽  
pp. 6036-6046 ◽  
Author(s):  
Liza Nielsen ◽  
Ritu Khurana ◽  
Alisa Coats ◽  
Sven Frokjaer ◽  
Jens Brange ◽  
...  
Keyword(s):  
Environmental Factors ◽  
Molecular Mechanism ◽  
Fibril Formation ◽  
Kinetics Of
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