More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display.
Journal
RSC advances
ISSN: 2046-2069
Titre abrégé: RSC Adv
Pays: England
ID NLM: 101581657
Informations de publication
Date de publication:
15 Oct 2020
15 Oct 2020
Historique:
received:
13
08
2020
accepted:
12
10
2020
entrez:
6
5
2022
pubmed:
21
10
2020
medline:
21
10
2020
Statut:
epublish
Résumé
Herein, we report a high-throughput approach for the selection of peripheral protein domains that bind specifically to cholesterol in lipid membranes. We discovered variants of perfringolysin O, with non-conserved amino acid substitutions at regions crucial for cholesterol recognition, demonstrating an unprecedented amino acid sequence variability with binding ability for cholesterol. The developed approach provides an effective platform for a comprehensive study of protein lipid interactions.
Identifiants
pubmed: 35517550
doi: 10.1039/d0ra06976k
pii: d0ra06976k
pmc: PMC9057304
doi:
Types de publication
Journal Article
Langues
eng
Pagination
38678-38682Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
There are no conflicts of interest to declare.
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