scholarly journals Gold nanocolloid–protein interactions and their impact on β-sheet amyloid fibril formation

RSC Advances ◽  
2018 ◽  
Vol 8 (2) ◽  
pp. 980-986 ◽  
Author(s):  
Heloise R. Barros ◽  
Maria Kokkinopoulou ◽  
Izabel C. Riegel-Vidotti ◽  
Katharina Landfester ◽  
Héloïse Thérien-Aubin
Keyword(s):  
Protein Interactions ◽  
Amyloid Fibril ◽  
Interaction Mechanism ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Degenerative Diseases ◽  
Amyloid Fibril Formation ◽  
Protein Fibrils ◽  
Β Sheet

Formation of amyloid protein fibrils is associated with degenerative diseases. Here, the interaction mechanism between globular and fibrillar proteins with AuNPs were investigated in order to potentially control and reverse the fibrillation process.

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.

Cetyltrimethylammonium bromide (CTAB) promote amyloid fibril formation in carbohydrate binding protein (concanavalin A) at physiological pH

RSC Advances ◽  
2016 ◽  
Vol 6 (44) ◽  
pp. 38100-38111 ◽  
Author(s):  
Javed Masood Khan ◽  
Mohd Shahnawaz Khan ◽  
Mohd Sajid Ali ◽  
Nasser Abdulatif Al-Shabib ◽  
Rizwan Hasan Khan
Keyword(s):  
Concanavalin A ◽  
Cetyltrimethylammonium Bromide ◽  
Amyloid Fibril ◽  
Alpha Helix ◽  
Fibril Formation ◽  
Carbohydrate Binding ◽  
Con A ◽  
Amyloid Fibril Formation ◽  
High Concentrations ◽  
Β Sheet

Low concentration of CTAB provoked cross β-sheet formation whereas high concentrations of CTAB direct to alpha helix induction in Con A.

scholarly journals Appearance of annular ring-like intermediates during amyloid fibril formation from human serum albumin

2015 ◽  
Vol 17 (35) ◽  
pp. 22862-22871 ◽  
Author(s):  
Shruti Arya ◽  
Arpana Kumari ◽  
Vijit Dalal ◽  
Mily Bhattacharya ◽  
Samrat Mukhopadhyay
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amyloid Fibril ◽  
Temporal Evolution ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Amyloid Assembly ◽  
Conformational Conversion ◽  
Β Sheet

A profound conformational conversion coupled with the temporal evolution of morphologically-distinct ring-like nanoscopic intermediates were monitored during the amyloid assembly of human serum albumin into β-sheet-rich fibrils.

The N-Terminal Repeat Domain of α-Synuclein Inhibits β-Sheet and Amyloid Fibril Formation†

Biochemistry ◽  
2003 ◽  
Vol 42 (3) ◽  
pp. 672-678 ◽  
Author(s):  
Jeffrey C. Kessler ◽  
Jean-Christophe Rochet ◽  
Peter T. Lansbury
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Terminal Repeat ◽  
Amyloid Fibril Formation ◽  
Repeat Domain ◽  
Β Sheet
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