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 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 Effect of Association State and Conformational Stability on the Kinetics of Immunoglobulin Light Chain Amyloid Fibril Formation at Physiological pH

2002 ◽  
Vol 277 (15) ◽  
pp. 12657-12665 ◽  
Author(s):  
Pierre O. Souillac ◽  
Vladimir N. Uversky ◽  
Ian S. Millett ◽  
Ritu Khurana ◽  
Sebastian Doniach ◽  
...  
Keyword(s):  
Light Chain ◽  
Amyloid Fibril ◽  
Conformational Stability ◽  
Fibril Formation ◽  
Immunoglobulin Light Chain ◽  
Amyloid Fibril Formation ◽  
Kinetics Of ◽  
Association State

Early Kinetics of Amyloid Fibril Formation Reveals Conformational Reorganisation of Initial Aggregates

2007 ◽  
Vol 366 (4) ◽  
pp. 1351-1363 ◽  
Author(s):  
N. Cerdà-Costa ◽  
A. Esteras-Chopo ◽  
F.X. Avilés ◽  
L. Serrano ◽  
V. Villegas
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Kinetics Of

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

Elucidating the Kinetics of β-Amyloid Fibril Formation

2005 ◽  
pp. 106-118 ◽  
Author(s):  
Nadia J. Edwin ◽  
Grigor B. Bantchev ◽  
Paul S. Russo ◽  
Robert P. Hammer ◽  
Robin L. McCarley
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Kinetics Of

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

scholarly journals Structural development of amyloid precursors in insulin B chain and the inhibition effect by fibrinogen

2021 ◽  
Author(s):  
Naoki Yamamoto ◽  
Rintaro Inoue ◽  
Yoshiteru Makino ◽  
Naoya Shibayama ◽  
Akira Naito ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Size Exclusion ◽  
Inhibition Mechanism ◽  
Structural Development ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Exclusion Chromatography ◽  
The Stability

Amyloid fibrils are abnormal protein aggregates that relate to a large number of amyloidoses and neurodegenerative diseases. The oligomeric precursors, or prefibrillar intermediates, which emerge prior to the amyloid fibril formation, have been known to play a crucial role for the formation. Therefore, it is essential to elucidate the mechanisms of the structural development of the prefibrillar intermediates and ways to prevent its fibril formation. An insulin-derived peptide, insulin B chain, has been known for its stable accumulation of the prefibrillar intermediates. In this study, structural development of B chain prefibrillar intermediates was monitored by transmission electron microscopy and small-angle X-ray scattering combined with size exclusion chromatography and solid-state NMR spectroscopy to elucidate the stability and secondary structure. We further tracked its inhibition process by fibrinogen (Fg), which has been known to effectively prevent the amyloid fibril formation of B chain. We demonstrated that prefibrillar intermediates are wavy structures with low β-sheet content, growing in a multistep manner toward the nucleation for the amyloid fibril formation. In the presence of Fg, the formation of the prefibrillar intermediates slowed down by forming specific complexes. These observations suggest that the prefibrillar intermediates serve as reaction fields for the nucleation and its propagation for the amyloid fibril formation, whereas the inhibition of prefibrillar intermediate elongation by Fg is the significant factor to suppress the fibril formation. We propose that the obtained molecular picture could be a general inhibition mechanism of the amyloid fibril formation by the 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.

The Influence of Ca2+ and Zn2+ on the Amyloid Fibril Formation by β-Casein

2020 ◽  
Vol 27 (9) ◽  
pp. 915-922
Author(s):  
Jia Wang ◽  
Jihua Liu ◽  
Guangguang Du ◽  
Yang An ◽  
Chunfang Zhao ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Intrinsic Fluorescence ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Concentration Changes ◽  
Set Up ◽  
The Relationship ◽  
Different Tissues

Background: The amyloid fibril formation in different tissues or organs is related to amyloidosis. The Ca2+, Zn2+ and heparan sulfate (HS) are important elements and compositions in human body, which play a key role in regulating various physiological activities. Recently, there are increasing evidence suggest that they are closely linked to the amyloid fibril formation. Objective: The effect of Ca2+ and Zn2+ on the amyloid fibril formation by β-casein was investigated in the absence and presence of HS, which was significantly to explore the relationship between the concentration changes of Ca2+ and Zn2+ and amyloid fibril formation. Method: In this work, the influence of Ca2+ and Zn2+ on the β-casein fibril formation in the absence and presence of HS was investigated by various methods of Thioflavin T fluorescence assay, transmission electron microscopy and intrinsic fluorescence measure. Results: The results demonstrated that Ca2+ and Zn2+ promoted the β-casein fibril formation. The effect of Ca2+ was greater than that of Zn2+. Meanwhile, the both metal ions had stronger effects when β-casein was incubated with HS together. In addition, it was also observed that the microenvironment of β-casein was changed because the intrinsic fluorescence peaks were red-shifted on the influence of Ca2+ and Zn2+. Conclusion: Ca2+ and Zn2+ were capable of promoting the β-casein fibril formation in the both absence and presence of HS. This work set up the foundation for further researching of the amyloidosis pathogenesis and provided new insight for us to understand relationship between the inflammation and amyloidosis.

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