scholarly journals Metal-dependent inhibition of amyloid fibril formation: synergistic effects of cobalt–tannic acid networks

Nanoscale ◽  
2019 ◽  
Vol 11 (4) ◽  
pp. 1921-1928 ◽  
Author(s):  
Wenjie Zhang ◽  
Andrew J. Christofferson ◽  
Quinn A. Besford ◽  
Joseph J. Richardson ◽  
Junling Guo ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Tannic Acid ◽  
Amyloid Fibril ◽  
Synergistic Effects ◽  
Fibril Formation ◽  
Coated Particles ◽  
Amyloid Fibril Formation ◽  
Dependent Inhibition

Cobalt–tannic acid-coated gold nanoparticles are found to better inhibit amyloid fibril formation than other metal-based tannic acid-coated particles.

Amyloid fibril formation by β-lactoglobulin is inhibited by gold nanoparticles

2014 ◽  
Vol 69 ◽  
pp. 137-145 ◽  
Author(s):  
Subrata Sardar ◽  
Sampa Pal ◽  
Sanhita Maity ◽  
Jishnu Chakraborty ◽  
Umesh Chandra Halder
Keyword(s):  
Gold Nanoparticles ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Lactoglobulin

scholarly journals Antioxidants From the Class of Polyphenols, NAC and Vitamin C Act Differently on Amyloid Fibril Formation by Two Human Cystatins: Stefin B and Cystatin C.

2020 ◽  
Author(s):  
Alma Jahic Mujkic ◽  
Samra Hasanbasic ◽  
Magda Tušek Žnidarič ◽  
Selma Berbic ◽  
Eva Zerovnik
Keyword(s):  
Vitamin C ◽  
Cystatin C ◽  
Amyloid Fibril ◽  
Synergistic Effects ◽  
Fibril Formation ◽  
Homologous Proteins ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Amyloid Fibrillation ◽  
Anti Oxidant

We compare the effect on amyloid fibril formation by two homologous proteins from the family of cystatins, human stefin B (stB) and cystatin C (cysC) in presence of 3 polyphenols: curcumin, resveratrol and quercetin and 2 non-phenolic anti-oxidants: vitamin C (VitC) and N-acetyl cystein (NAC). Some of the experimental data have already been presented, here we compare, further discuss and highlight the results. The amyloid fibril formation was followed by ThT fluorescence and transmission electron microscopy. Inhibitory effects on amyloid fibrillation reaction depended on anti-oxidant class and concentration. The fact that different effect of polyphenols was observed with the two cystatins; Cur acted inhibitory on stB but not on cysC fibril formation, could be explained if the 3 polyphenols would not bind to the same binding site in the fibrils core. Other differences are pointed out and discussed. Synergistic effects of VitC and chosen polyphenols on amyloid fibrilllation of human stB have been explored and are reported here for the first time.

scholarly journals Tannic Acid Inhibits α-Synuclein Amyloid Fibril Formation via Binding to the Monomer N-terminal Domain

2021 ◽  
Author(s):  
Jonathan Stoeber ◽  
Jonathan K Williams ◽  
Prabhas V. Moghe ◽  
Jean Baum
Keyword(s):  
Tannic Acid ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Critical Role ◽  
Intrinsically Disordered Protein ◽  
Fibril Formation ◽  
Dependent Manner ◽  
Intrinsically Disordered ◽  
Terminal Domain ◽  
Amyloid Fibril Formation

α-Synuclein (αS) is an intrinsically disordered protein (IDP) that aggregates into amyloid fibrils during the progression of Parkinson's Disease and other synucleinopathies. The N-terminal domain (residues 1-60) is now understood to play a critical role in the initial nucleation of aggregation, as well as a pivotal role in the monomer-fibril interaction underlying amyloid seeding. Here we report on the interaction between αS and the polyphenol tannic acid (TA), where a combination of solution NMR, atomic force microscopy (AFM), and ThT assays have identified that TA targets the αS N-terminal domain to inhibit amyloid fibril formation in a pH dependent manner. This work highlights the importance of targeting the N-terminus of αS to arrest fibril formation, and suggests the importance of including polyphenolic moieties in future amyloid inhibitors.

scholarly journals Citrate stabilized gold nanoparticles interfere with amyloid fibril formation: D76N and ΔN6 β2-microglobulin variants

Nanoscale ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 4793-4806 ◽  
Author(s):  
Giorgia Brancolini ◽  
Maria Celeste Maschio ◽  
Cristina Cantarutti ◽  
Alessandra Corazza ◽  
Federico Fogolari ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Amyloid Fibril Formation

Mechanism for how citrate covered gold NP influence protein aggregation and thus fibril formation for the highly amyloidogenic variants D76N and ΔN6 β2-microglobulin.

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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