Send to

Choose Destination
Chembiochem. 2019 Dec 9. doi: 10.1002/cbic.201900655. [Epub ahead of print]

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

Author information

Department of Biochemistry, Groningen Biomolecular Sciences and, Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Department of Biomolecular Chemistry and Catalysis, Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
DWI Leibniz Institute for Interactive Materials, Forckenbeckstrasse 50, 52074, Aachen, Germany.


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 (Lo ) and liquid-disordered (Ld ) 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 Ld phase. These data demonstrate that the Lo domain in model membranes is highly unfavorable for a single membrane-spanning peptide.


biological membranes; lipid phase separation; membrane partitioning; palmitoylation; trifunctional linker


Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center