Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation?

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 specifi...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2020-08, Vol.56 (68), p.9787-979
Hauptverfasser: Lam, Yuko P. Y, Chiu, Cookson K. C, Wootton, Christopher A, Hands-Portman, Ian, Li, Meng, Barrow, Mark P, O'Connor, Peter B
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container_end_page 979
container_issue 68
container_start_page 9787
container_title Chemical communications (Cambridge, England)
container_volume 56
creator Lam, Yuko P. Y
Chiu, Cookson K. C
Wootton, Christopher A
Hands-Portman, Ian
Li, Meng
Barrow, Mark P
O'Connor, Peter B
description 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. A diagram to show the differences between wild-type and deamidated hIAPPs interaction with site specific and non-specific inhibitors.
doi_str_mv 10.1039/d0cc03548c
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source MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection
subjects Amino Acid Sequence
Amyloid - chemistry
Amyloid - metabolism
Catechin - analogs & derivatives
Catechin - chemistry
Catechin - metabolism
Catechin - pharmacology
Humans
Inhibitors
Islet Amyloid Polypeptide - chemistry
Islet Amyloid Polypeptide - metabolism
Microscopy, Electron, Transmission
Protein Aggregates - drug effects
Proteins
Spectrometry, Fluorescence
title Does deamidation affect inhibitory mechanisms towards amyloid protein aggregation?
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