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Acyl transfer from membrane lipids to peptides is a generic process.

Dods, R.H. and Bechinger, B. and Mosely, J.A. and Sanderson, J.M. (2013) 'Acyl transfer from membrane lipids to peptides is a generic process.', Journal of molecular biology., 425 (22). pp. 4379-4387.

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.

Item Type:Article
Keywords:Phospholipid, Membrane, Acylation, Lipidation, Melittin.
Full text:(AM) Accepted Manuscript
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Status:Peer-reviewed
Publisher Web site:http://dx.doi.org/10.1016/j.jmb.2013.07.013
Publisher 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
Date accepted:No date available
Date deposited:21 February 2014
Date of first online publication:November 2013
Date first made open access:No date available

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