Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation?

Autor:	Lam YPY; Department of Chemistry, University of Warwick, Coventry, UK. p.oconnor@warwick.ac.uk., Chiu CKC; Department of Chemistry, University of Warwick, Coventry, UK. p.oconnor@warwick.ac.uk., Wootton CA; Department of Chemistry, University of Warwick, Coventry, UK. p.oconnor@warwick.ac.uk., Hands-Portman I; Department of Life Sciences, University of Warwick, Coventry, UK., Li M; Department of Chemistry, University of Warwick, Coventry, UK. p.oconnor@warwick.ac.uk., Barrow MP; Department of Chemistry, University of Warwick, Coventry, UK. p.oconnor@warwick.ac.uk., O'Connor PB; Department of Chemistry, University of Warwick, Coventry, UK. p.oconnor@warwick.ac.uk.
Jazyk:	angličtina
Zdroj:	Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2020 Aug 25; Vol. 56 (68), pp. 9787-9790.
DOI:	10.1039/d0cc03548c
Abstrakt:	Deamidated amyloid proteins have been shown to accelerate fibril formation. Herein, the results show the inhibition performance and the interaction site between site-specific inhibitor and amyloid protein are significantly influenced by deamidation; while the inhibition mechanism of non-site specific inhibitor shows no significant disruption caused by amyloid protein deamidation.
Databáze:	MEDLINE
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