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. Thedeveloped approach provides an effective platform for a comprehensive study of protein lipid interactions.
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CITATION STYLE
Šakanović, A., Kranjc, N., Omersa, N., Podobnik, M., & Anderluh, G. (2020). More than one way to bind to cholesterol: Atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display. RSC Advances, 10(63), 38678–38682. https://doi.org/10.1039/d0ra06976k
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