Understanding and modelling the interactions of peptides with membranes: from partitioning to self-assembly.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
04 2020
04 2020
Historique:
received:
18
10
2019
revised:
27
12
2019
accepted:
28
12
2019
pubmed:
2
2
2020
medline:
8
6
2021
entrez:
2
2
2020
Statut:
ppublish
Résumé
Atomic detail simulations are starting to reveal how flexible polypeptides interact with fluid lipid bilayers. These insights are transforming our understanding of one of the fundamental processes in biology: membrane protein folding and assembly. Advanced molecular dynamics (MD) simulation techniques enable accurate prediction of protein structure, folding pathways and assembly in microsecond-timescales. Such simulations show how membrane-active peptides self-assemble in cell membranes, revealing their binding, folding, insertion, and aggregation, while at the same time providing atomic resolution details of peptide-lipid interactions. Essential to the impact of simulations are experimental approaches that enable calibration and validation of the computational models and techniques. In this review, we summarize the current development of applying unbiased atomic detail MD simulations and the relation to experimental techniques, to study peptide folding and provide our perspective of the field.
Identifiants
pubmed: 32006812
pii: S0959-440X(19)30160-5
doi: 10.1016/j.sbi.2019.12.021
pii:
doi:
Substances chimiques
Amyloid
0
Ion Channels
0
Peptides
0
Solutions
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
160-166Informations de copyright
Copyright © 2019. Published by Elsevier Ltd.