ChemInform Abstract: Construction of Peptides that Undergo Structural Transition from α-Helix to β-Sheet and Amyloid Fibril Formation by the Introduction of N-Terminal Hydrophobic Amino Acids.

ChemInform ◽  
2000 ◽  
Vol 31 (49) ◽  
pp. no-no
Author(s):  
Yuta Takahashi ◽  
Taro Yamashita ◽  
Akihiko Ueno ◽  
Hisakazu Mihara
Keyword(s):  
Amino Acids ◽  
Structural Transition ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Hydrophobic Amino Acids ◽  
Α Helix ◽  
Β Sheet

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.

Sulfated polysaccharide ascophyllan prevents amyloid fibril formation of human insulin and inhibits amyloid-induced hemolysis and cytotoxicity in PC12 cells

2021 ◽  
Author(s):  
Yan Liang ◽  
Mikinori Ueno ◽  
Shijiao Zha ◽  
Takasi Okimura ◽  
Zedong Jiang ◽  
...  
Keyword(s):  
Pc12 Cells ◽  
Human Insulin ◽  
Amyloid Fibril ◽  
Gel Filtration ◽  
Sulfated Polysaccharide ◽  
Fibril Formation ◽  
Sulfated Polysaccharides ◽  
Structure Transition ◽  
Amyloid Fibril Formation ◽  
Α Helix

Abstract We found that ascophyllan significantly inhibited the fibrillation of human insulin, and was the most effective among the sulfated polysaccharides tested. Gel-filtration analysis suggested that ascophyllan was capable of forming a complex with insulin through a weak interaction. Secondary structure transition from native α-helix to β-sheet predominant structure of insulin under the fibrillation conditions was suppressed in the presence of ascophyllan. Interestingly, ascophyllan attenuated insulin fibrils-induced hemolysis of human erythrocytes. Moreover ascophyllan attenuated insulin amyloid induced cytotoxicity on rat pheochromocytoma PC12 cells and reduced the level of intracellular reactive oxygen species (ROS). This is the first report indicating that a sulfated polysaccharide, ascophyllan can suppress the insulin amyloid fibril formation and inhibit the fibril-induced detrimental bioactivities.

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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