Skip to main content

Research Repository

Advanced Search

Acyl Transfer from Membrane Lipids to Peptides Is a Generic Process

Dods, RH; Bechinger, B; Mosely, JA; Sanderson, JM

Acyl Transfer from Membrane Lipids to Peptides Is a Generic Process Thumbnail


Authors

RH Dods

B Bechinger

JA Mosely



Abstract

The generality of acyl transfer from phospholipids to membrane-active peptides has been probed using liquid chromatography–mass spectrometry analysis of peptide–lipid mixtures. The peptides examined include melittin, magainin II, PGLa, LAK1, LAK3 and penetratin. Peptides were added to liposomes with membrane lipid compositions ranging from pure phosphatidylcholine (PC) to mixtures of PC with phosphatidylethanolamine, phosphatidylserine or phosphatidylglycerol. Experiments were typically conducted at pH 7.4 at modest salt concentrations (90 mM NaCl). In favorable cases, lipidated peptides were further characterized by tandem mass spectrometry methods to determine the sites of acylation. Melittin and magainin II were the most reactive peptides, with significant acyl transfer detected under all conditions and membrane compositions. Both peptides were lipidated at the N-terminus by transfer from PC, phosphatidylethanolamine, phosphatidylserine or phosphatidylglycerol, as well as at internal sites: lysine for melittin; serine and lysine for magainin II. Acyl transfer could be detected within 3 h of melittin addition to negatively charged membranes. The other peptides were less reactive, but for each peptide, acylation was found to occur in at least one of the conditions examined. The data demonstrate that acyl transfer is a generic process for peptides bound to membranes composed of diacylglycerophospholipids. Phospholipid membranes cannot therefore be considered as chemically inert toward peptides and by extension proteins.

Citation

Dods, R., Bechinger, B., Mosely, J., & Sanderson, J. (2013). Acyl Transfer from Membrane Lipids to Peptides Is a Generic Process. Journal of Molecular Biology, 425(22), 4379-4387. https://doi.org/10.1016/j.jmb.2013.07.013

Journal Article Type Article
Publication Date Nov 1, 2013
Deposit Date Sep 15, 2013
Publicly Available Date Feb 21, 2014
Journal Journal of Molecular Biology
Print ISSN 0022-2836
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 425
Issue 22
Pages 4379-4387
DOI https://doi.org/10.1016/j.jmb.2013.07.013
Keywords Phospholipid, Membrane, Acylation, Lipidation, Melittin.
Public URL https://durham-repository.worktribe.com/output/1469865

Files

Accepted Journal Article (999 Kb)
PDF

Copyright Statement
NOTICE: this is the author’s version of a work that was accepted for publication in Journal of molecular biology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of molecular biology, 425, 22, 2013, 10.1016/j.jmb.2013.07.013






You might also like



Downloadable Citations