Interaction of Human Resistin with Human Islet Amyloid Polypeptide at Charged Phospholipid Membranes.
Journal
ACS omega
ISSN: 2470-1343
Titre abrégé: ACS Omega
Pays: United States
ID NLM: 101691658
Informations de publication
Date de publication:
05 Jul 2022
05 Jul 2022
Historique:
received:
07
03
2022
accepted:
19
05
2022
entrez:
11
7
2022
pubmed:
12
7
2022
medline:
12
7
2022
Statut:
epublish
Résumé
An X-ray reflectivity study on the interaction of recombinant human resistin (hRes) with fibrillation-prone human islet amyloid polypeptide (hIAPP) at anionic phospholipid Langmuir films as model membranes is presented. Aggregation and amyloid formation of hIAPP is considered the main mechanism of pancreatic β-cell loss in patients with type 2 diabetes mellitus. Resistin shows a chaperone-like ability, but also tends to form aggregates by itself. Resistin and hIAPP cross multiply metabolism pathways. In this study, we researched the potential protective effects of resistin against hIAPP-induced lipid membrane rupture. The results demonstrate that resistin can inhibit or prevent hIAPP adsorption even in the presence of aggregation-promoting negatively charged lipid interfaces. Moreover, we found strong hydrophobic interactions of resistin at the bare buffer-air interface.
Identifiants
pubmed: 35811869
doi: 10.1021/acsomega.2c01363
pmc: PMC9260898
doi:
Types de publication
Journal Article
Langues
eng
Pagination
22377-22382Informations de copyright
© 2022 The Authors. Published by American Chemical Society.
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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