Capsaicin-Coated Silver Nanoparticles Inhibit Amyloid Fibril Formation of Serum Albumin

Biochemistry ◽  
2016 ◽  
Vol 55 (24) ◽  
pp. 3345-3348 ◽  
Author(s):  
Bibin G. Anand ◽  
Kriti Dubey ◽  
Dolat Singh Shekhawat ◽  
Karunakar Kar
Keyword(s):  
Silver Nanoparticles ◽  
Serum Albumin ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Oxidation Enhances Human Serum Albumin Thermal Stability and Changes the Routes of Amyloid Fibril Formation

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e84552 ◽  
Author(s):  
Giuseppe Sancataldo ◽  
Valeria Vetri ◽  
Vito Foderà ◽  
Gianluca Di Cara ◽  
Valeria Militello ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

Amyloid Fibril Formation and Other Aggregate Species Formed by Human Serum Albumin Association

2006 ◽  
Vol 110 (42) ◽  
pp. 20733-20736 ◽  
Author(s):  
Pablo Taboada ◽  
Silvia Barbosa ◽  
Emilio Castro ◽  
Víctor Mosquera
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

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.

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

scholarly journals Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners

2021 ◽  
Vol 296 ◽  
pp. 100510
Author(s):  
Keiichi Yamaguchi ◽  
Masatomo So ◽  
César Aguirre ◽  
Kensuke Ikenaka ◽  
Hideki Mochizuki ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation
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