Pristine and Hydroxylated Fullerenes Prevent the Aggregation of Human Islet Amyloid Polypeptide and Display Different Inhibitory Mechanisms.

C60 hIAPP aggregation inhibitory mechanism replica exchange molecular dynamics simulations type 2 diabetes

Journal

Frontiers in chemistry
ISSN: 2296-2646
Titre abrégé: Front Chem
Pays: Switzerland
ID NLM: 101627988

Informations de publication

Date de publication:
2020
Historique:
received: 31 10 2019
accepted: 16 01 2020
entrez: 3 3 2020
pubmed: 3 3 2020
medline: 3 3 2020
Statut: epublish

Résumé

Protein aggregation, involving the formation of dimers, oligomers, and fibrils, is associated with many human diseases. Type 2 diabetes is one of the common amyloidosis and linked with the aggregation of human islet amyloid polypeptide (hIAPP). A series of nanoparticles are reported to be able to interact with proteins and enhance/inhibit protein aggregation. However, the effects of C

Identifiants

pubmed: 32117877
doi: 10.3389/fchem.2020.00051
pmc: PMC7013002
doi:

Types de publication

Journal Article

Langues

eng

Pagination

51

Informations de copyright

Copyright © 2020 Bai, Lao, Chen, Tang and Wei.

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Auteurs

Cuiqin Bai (C)

State Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.

Zenghui Lao (Z)

State Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.

Yujie Chen (Y)

State Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.

Yiming Tang (Y)

State Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.

Guanghong Wei (G)

State Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.

Classifications MeSH