A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes.
biological membranes
lipid phase separation
membrane partitioning
palmitoylation
trifunctional linker
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
04 05 2020
04 05 2020
Historique:
received:
29
10
2019
pubmed:
10
12
2019
medline:
29
5
2021
entrez:
10
12
2019
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 31814256
doi: 10.1002/cbic.201900655
pmc: PMC7317724
doi:
Substances chimiques
Lipid Bilayers
0
Peptide Fragments
0
Proteins
0
Unilamellar Liposomes
0
Palmitic Acid
2V16EO95H1
Tyrosine
42HK56048U
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1320-1328Informations de copyright
© 2019 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
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