SDS modulates amyloid fibril formation and conformational change in succinyl-ConA at low pH

2021 ◽  
pp. 120494
Author(s):  
Javed Masood Khan ◽  
Ajamaluddin Malik ◽  
Mohammad Z Ahmed ◽  
Anwar Ahmed
Keyword(s):  
Conformational Change ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Low Ph ◽  
Amyloid Fibril Formation

Ion Mobility Mass Spectrometry Studies of the Inhibition of Alpha Synuclein Amyloid Fibril Formation by ( - )-Epigallocatechin-3-Gallate

2011 ◽  
Vol 64 (1) ◽  
pp. 36 ◽  
Author(s):  
Yanqin Liu ◽  
Lam H. Ho ◽  
John. A. Carver ◽  
Tara L. Pukala
Keyword(s):  
Mass Spectrometry ◽  
Conformational Change ◽  
Ion Mobility ◽  
Amyloid Fibril ◽  
Heterogeneous Systems ◽  
Alpha Synuclein ◽  
Fibril Formation ◽  
Ion Mobility Mass Spectrometry ◽  
Compact Structure ◽  
Amyloid Fibril Formation

Ion mobility-mass spectrometry (IM-MS) is emerging as an important biophysical technique for the structural analysis of proteins and their assemblies, in particular for structurally heterogeneous systems such as those on the protein misfolding and aggregation pathway. Using IM-MS we have monitored amyloid fibril formation of A53T α-synuclein, a mutant synuclein protein associated with Parkinson’s disease, and identified that a conformational change towards a more compact structure occurs during the initial stages of aggregation. Binding of A53T α-synuclein to a flavenoid based amyloid fibril inhibitor, (–)-epigallocatechin-3-gallate, has been observed with a 1:1 stoichiometry. By analysis of ion collision cross-sections, we show epigallocatechin gallate binding prevents protein conformational change, and in turn decreases the formation of fibrillar aggregates.

Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH

2014 ◽  
Vol 70 ◽  
pp. 214-221 ◽  
Author(s):  
Jarosław Wawer ◽  
Joanna Krakowiak ◽  
Michał Szociński ◽  
Zofia Lustig ◽  
Marcin Olszewski ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Egg White ◽  
Fibril Formation ◽  
Low Ph ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Amyloid Fibril Formation ◽  
Hen Egg White ◽  
Hen Egg

Monitoring of the Surface Tension by the Pendant Drop Technique for Detection of Insulin Fibrillogenesis

2021 ◽  
Author(s):  
Katarina Siposova ◽  
Dagmar Sedlakova ◽  
Andrey Musatov
Keyword(s):  
Surface Tension ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Low Ph ◽  
Pendant Drop ◽  
Amyloid Fibril Formation ◽  
Ph Buffer ◽  
Drop Technique

Monitoring of aggregation of amyloid-prone proteins is critical for understanding of the mechanism of amyloid fibril formation. Insulin, when dissolved in low pH buffer has a surface tension of 61-64...

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.

Monitoring the prevention of amyloid fibril formation by α-crystallin

FEBS Journal ◽  
2007 ◽  
Vol 274 (24) ◽  
pp. 6290-6304 ◽  
Author(s):  
Agata Rekas ◽  
Lucy Jankova ◽  
David C. Thorn ◽  
Roberto Cappai ◽  
John A. Carver
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation
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