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 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.

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 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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