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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.
Sakanovic, Aleksandra; Kranjc, Nace; Omersa, Neza; Podobnik, Marjetka; Anderluh, Gregor.
Afiliação
  • Sakanovic A; Department of Molecular Biology and Nanobiotechnology, National Institute of Chemistry Ljubljana Slovenia gregor.anderluh@ki.si.
  • Kranjc N; Biosciences Doctoral Program, Biotechnical Faculty, University of Ljubljana Ljubljana Slovenia.
  • Omersa N; Department of Molecular Biology and Nanobiotechnology, National Institute of Chemistry Ljubljana Slovenia gregor.anderluh@ki.si.
  • Podobnik M; Department of Molecular Biology and Nanobiotechnology, National Institute of Chemistry Ljubljana Slovenia gregor.anderluh@ki.si.
  • Anderluh G; Department of Molecular Biology and Nanobiotechnology, National Institute of Chemistry Ljubljana Slovenia gregor.anderluh@ki.si.
RSC Adv ; 10(63): 38678-38682, 2020 Oct 15.
Article em En | MEDLINE | ID: mdl-35517550
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.

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Idioma: En Ano de publicação: 2020 Tipo de documento: Article