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Title:The effect of three polyphenols and some other anti-oxidant substances on amyloid fibril formation by human cystatin C
Authors:ID Jahić, Alma (Author)
ID Tušek-Žnidarič, Magda (Author)
ID Pintar, Sara (Author)
ID Berbić, Selma (Author)
ID Žerovnik, Eva (Author)
Files:URL URL - Source URL, visit http://dx.doi.org/10.1016/j.neuint.2020.104806
 
.pdf PDF - Presentation file, download (7,93 MB)
MD5: AE8CB27FCAB7F417731B068312F84F37
 
Language:English
Typology:1.01 - Original Scientific Article
Organization:Logo NIB - National Institute of Biology
Abstract:Human cystatin C (CysC) is an amyloid forming protein involved in the hereditary cerebral amyloid angiopathy (HCCAA) that affects arteries in the brain and the peripheral nervous system. In this study we measured the influence of several substances on human CysC aggregation and amyloid fibril formation, induced at pH 4 in vitro. The effect of three polyphenols: resveratrol, quercetin and curcumin and of two antioxidants: vitamin C (VitC) and N-acetyl-L-cysteine (NAC) was explored as well as the effect of sulphoraphane (SF) and α-lipoic acid (AL). The formation of amyloid fibrils was followed by Thioflavin T (ThT) fluorescence and by transmission electron microscopy (TEM). Effects on the length of the lag phase were revealed by following the increase of ThT fluorescence intensity with time. The amount and morphology of fibrils in comparison to prefibrillar aggregates and globular oligomers were evaluated by TEM at the plateau stage of the reaction. Thermal stabilization of the CysC monomer by the small compounds was measured by differential scanning fluorimetry (DSF). NAC, VitC and SF exhibited the largest inhibitory effect on amyloid fibril growth. The effects of polyphenols were not significant, apart from resveratrol, which partly inhibited the amyloid fibril growth.
Publication version:Version of Record
Publication date:01.11.2020
Year of publishing:2020
Number of pages:str. 1-9
Numbering:Vol. 140
PID:20.500.12556/DiRROS-19524 New window
UDC:577
ISSN on article:0197-0186
DOI:10.1016/j.neuint.2020.104806 New window
COBISS.SI-ID:26233859 New window
Publication date in DiRROS:22.07.2024
Views:318
Downloads:434
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Record is a part of a journal

Title:Neurochemistry International
Shortened title:Neurochem. int.
Publisher:Pergamon Press
ISSN:0197-0186
COBISS.SI-ID:26012928 New window

Document is financed by a project

Funder:ARIS - Slovenian Research and Innovation Agency
Project number:P1-0140-2015
Name:Proteoliza in njena regulacija

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License:CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Link:http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.

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