Structural Dissection of the First Events Following Membrane Binding of the Islet Amyloid Polypeptide.
amylin
amyloid aggregation
islet amyloid polypeptide
peptide-membrane interactions
type 2 diabetes mellitus
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2022
2022
Historique:
received:
06
01
2022
accepted:
18
02
2022
entrez:
4
4
2022
pubmed:
5
4
2022
medline:
5
4
2022
Statut:
epublish
Résumé
The islet amyloid polypeptide (IAPP) is the main constituent of the amyloid fibrils found in the pancreas of type 2 diabetes patients. The aggregation of IAPP is known to cause cell death, where the cell membrane plays a dual role: being a catalyst of IAPP aggregation and being the target of IAPP toxicity. Using ATR-FTIR spectroscopy, transmission electron microscopy, and molecular dynamics simulations we investigate the very first molecular steps following IAPP binding to a lipid membrane. In particular, we assess the combined effects of the charge state of amino-acid residue 18 and the IAPP-membrane interactions on the structures of monomeric and aggregated IAPP. Distinct IAPP-membrane interaction modes for the various IAPP variants are revealed. Membrane binding causes IAPP to fold into an amphipathic
Identifiants
pubmed: 35372496
doi: 10.3389/fmolb.2022.849979
pii: 849979
pmc: PMC8965455
doi:
Types de publication
Journal Article
Langues
eng
Pagination
849979Informations de copyright
Copyright © 2022 Khemtemourian, Fatafta, Davion, Lecomte, Castano and Strodel.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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