The polyphenolic phytoalexin polydatin inhibits amyloid aggregation of recombinant human prion protein
Author:
Affiliation:
1. School of Biotechnology
2. Jawaharlal Nehru University
3. New Delhi
4. India
5. Department of Biotechnology
6. School of Computational and Integrative Sciences
7. Special Centre of Systems Medicine
Abstract
Polydatin is found to be a pharmacologically-significant scaffold that can bind to the rPrPres repertoire and inhibit its conversion to the highly infectious and neurotoxic PrPSc-like form, thus acting like a promising anti-prion drug lead.
Funder
Indian Council of Medical Research
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2021/RA/D1RA01891D
Reference48 articles.
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