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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.

SUBMITTER: Sakanovic A 

PROVIDER: S-EPMC9057304 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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

Šakanović Aleksandra A   Kranjc Nace N   Omersa Neža N   Podobnik Marjetka M   Anderluh Gregor G  

RSC advances 20201021 63


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. ...[more]

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