Issue 63, 2020, Issue in Progress

More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display

Abstract

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.

Graphical abstract: More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display

Supplementary files

Article information

Article type
Paper
Submitted
13 Aug 2020
Accepted
12 Oct 2020
First published
21 Oct 2020
This article is Open Access
Creative Commons BY license

RSC Adv., 2020,10, 38678-38682

More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display

A. Šakanović, N. Kranjc, N. Omersa, M. Podobnik and G. Anderluh, RSC Adv., 2020, 10, 38678 DOI: 10.1039/D0RA06976K

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements