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A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes

Attachment of lipophilic groups is an important post‐translational modification of proteins, which involves the coupling of one or more anchors such as fatty acids, isoprenoids, phospholipids, or glycosylphosphatidyl inositols. To study its impact on the membrane partitioning of hydrophobic peptides...

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Autores principales: Syga, Łukasz, de Vries, Reinder H., van Oosterhout, Hugo, Bartelds, Rianne, Boersma, Arnold J., Roelfes, Gerard, Poolman, Bert
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7317724/
https://www.ncbi.nlm.nih.gov/pubmed/31814256
http://dx.doi.org/10.1002/cbic.201900655
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author Syga, Łukasz
de Vries, Reinder H.
van Oosterhout, Hugo
Bartelds, Rianne
Boersma, Arnold J.
Roelfes, Gerard
Poolman, Bert
author_facet Syga, Łukasz
de Vries, Reinder H.
van Oosterhout, Hugo
Bartelds, Rianne
Boersma, Arnold J.
Roelfes, Gerard
Poolman, Bert
author_sort Syga, Łukasz
collection PubMed
description Attachment of lipophilic groups is an important post‐translational modification of proteins, which involves the coupling of one or more anchors such as fatty acids, isoprenoids, phospholipids, or glycosylphosphatidyl inositols. To study its impact on the membrane partitioning of hydrophobic peptides or proteins, we designed a tyrosine‐based trifunctional linker. The linker allows the facile incorporation of two different functionalities at a cysteine residue in a single step. We determined the effect of the lipid modification on the membrane partitioning of the synthetic α‐helical model peptide WALP with or without here and in all cases below; palmitoyl groups in giant unilamellar vesicles that contain a liquid‐ordered (L(o)) and liquid‐disordered (L(d)) phase. Introduction of two palmitoyl groups did not alter the localization of the membrane peptides, nor did the membrane thickness or lipid composition. In all cases, the peptide was retained in the L(d) phase. These data demonstrate that the L(o) domain in model membranes is highly unfavorable for a single membrane‐spanning peptide.
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spelling pubmed-73177242020-06-29 A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes Syga, Łukasz de Vries, Reinder H. van Oosterhout, Hugo Bartelds, Rianne Boersma, Arnold J. Roelfes, Gerard Poolman, Bert Chembiochem Full Papers Attachment of lipophilic groups is an important post‐translational modification of proteins, which involves the coupling of one or more anchors such as fatty acids, isoprenoids, phospholipids, or glycosylphosphatidyl inositols. To study its impact on the membrane partitioning of hydrophobic peptides or proteins, we designed a tyrosine‐based trifunctional linker. The linker allows the facile incorporation of two different functionalities at a cysteine residue in a single step. We determined the effect of the lipid modification on the membrane partitioning of the synthetic α‐helical model peptide WALP with or without here and in all cases below; palmitoyl groups in giant unilamellar vesicles that contain a liquid‐ordered (L(o)) and liquid‐disordered (L(d)) phase. Introduction of two palmitoyl groups did not alter the localization of the membrane peptides, nor did the membrane thickness or lipid composition. In all cases, the peptide was retained in the L(d) phase. These data demonstrate that the L(o) domain in model membranes is highly unfavorable for a single membrane‐spanning peptide. John Wiley and Sons Inc. 2020-01-10 2020-05-04 /pmc/articles/PMC7317724/ /pubmed/31814256 http://dx.doi.org/10.1002/cbic.201900655 Text en © 2019 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Full Papers
Syga, Łukasz
de Vries, Reinder H.
van Oosterhout, Hugo
Bartelds, Rianne
Boersma, Arnold J.
Roelfes, Gerard
Poolman, Bert
A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes
title A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes
title_full A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes
title_fullStr A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes
title_full_unstemmed A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes
title_short A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes
title_sort trifunctional linker for palmitoylation and peptide and protein localization in biological membranes
topic Full Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7317724/
https://www.ncbi.nlm.nih.gov/pubmed/31814256
http://dx.doi.org/10.1002/cbic.201900655
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