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

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...

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Detalles Bibliográficos
Autores principales: Šakanović, Aleksandra, Kranjc, Nace, Omersa, Neža, Podobnik, Marjetka, Anderluh, Gregor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9057304/
https://www.ncbi.nlm.nih.gov/pubmed/35517550
http://dx.doi.org/10.1039/d0ra06976k
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author Šakanović, Aleksandra
Kranjc, Nace
Omersa, Neža
Podobnik, Marjetka
Anderluh, Gregor
author_facet Šakanović, Aleksandra
Kranjc, Nace
Omersa, Neža
Podobnik, Marjetka
Anderluh, Gregor
author_sort Šakanović, Aleksandra
collection PubMed
description 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.
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spelling pubmed-90573042022-05-04 More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display Šakanović, Aleksandra Kranjc, Nace Omersa, Neža Podobnik, Marjetka Anderluh, Gregor RSC Adv Chemistry 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. The Royal Society of Chemistry 2020-10-21 /pmc/articles/PMC9057304/ /pubmed/35517550 http://dx.doi.org/10.1039/d0ra06976k Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Šakanović, Aleksandra
Kranjc, Nace
Omersa, Neža
Podobnik, Marjetka
Anderluh, Gregor
More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display
title More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display
title_full More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display
title_fullStr More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display
title_full_unstemmed More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display
title_short More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display
title_sort more than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin o selected by ribosome display
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9057304/
https://www.ncbi.nlm.nih.gov/pubmed/35517550
http://dx.doi.org/10.1039/d0ra06976k
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