More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display. Issue 63 (21st October 2020)

• Record Type: Journal Article
• Authors: Šakanović, Aleksandra; Kranjc, Nace; Omersa, Neža; Podobnik, Marjetka; Anderluh, Gregor
• Is Part Of: RSC advances. Volume 10:Issue 63(2020)
• Page Start: 38678
• Page End: 38682
• Publication Date: 2020-10-21
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/d0ra06976k
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : By using developed ribosomal display, we discovered variants of perfringolysin O, a pore forming toxin from bacteria Clostridium perfringens, with non-conserved amino acid substitutions at regions crucial for cholesterol recognition. 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.