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.

scholarly journals Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin byAchromobacterProtease I

2001 ◽  
Vol 277 (2) ◽  
pp. 1310-1315 ◽  
Author(s):  
Gennady V. Kozhukh ◽  
Yoshihisa Hagihara ◽  
Toru Kawakami ◽  
Kazuhiro Hasegawa ◽  
Hironobu Naiki ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Amyloid Fibril Formation

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 Biophysical Studies on Protein Aggregation and Amyloid Fibril Formation

2012 ◽  
Vol 102 (3) ◽  
pp. 443a
Author(s):  
Mily Bhattacharya ◽  
Neha Jain ◽  
Priyanka Dogra ◽  
Soumyadyuti Samai ◽  
Smita Patil ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Biophysical Studies

scholarly journals Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH

2019 ◽  
Vol 294 (43) ◽  
pp. 15826-15835 ◽  
Author(s):  
Masahiro Noji ◽  
Kenji Sasahara ◽  
Keiichi Yamaguchi ◽  
Masatomo So ◽  
Kazumasa Sakurai ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Neutral Ph ◽  
Amyloid Fibril Formation

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.

Protein Aggregation and Amyloid Fibril Formation by an SH3 Domain Probed by Limited Proteolysis

2003 ◽  
Vol 334 (1) ◽  
pp. 129-141 ◽  
Author(s):  
Patrizia Polverino de Laureto ◽  
Niccolò Taddei ◽  
Erica Frare ◽  
Cristina Capanni ◽  
Silvia Costantini ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Limited Proteolysis ◽  
Sh3 Domain ◽  
Fibril Formation ◽  
Amyloid Fibril Formation
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