By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators discuss new findings in Peptides and Proteins. According to news reporting originating in Strasbourg, France, by NewsRx journalists, research stated, "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, nnagainin II, PGLa, LAK1, LAK3 and penetratin."
The news reporters obtained a quote from the research from the University of Strasbourg, "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."
According to the news reporters, the research concluded: "Phospholipid membranes cannot therefore be considered as chemically inert toward peptides and by extension proteins."
For more information on this research see: Acyl Transfer from Membrane Lipids to Peptides Is a Generic Process. Journal of Molecular Biology, 2013;425(22):4379-4387. Journal of Molecular Biology can be contacted at: Academic Press Ltd- Elsevier Science Ltd, 24-28 Oval Rd, London NW1 7DX, England. (Elsevier - www.elsevier.com; Journal of Molecular Biology - www.elsevier.com/wps/product/cws_home/622890)
Our news correspondents report that additional information may be obtained by contacting R.H. Dods, Univ Strasbourg, CNRS, Int Center Frontier Res Chem, Membrane Biophys & NMRChem InstUMR 7177, F-67000 Strasbourg, France. Additional authors for this research include B. Bechinger, J.A. Mosely and J.M. Sanderson (see also Peptides and Proteins).
Keywords for this news article include: France, Europe, Strasbourg, Amino Acids, Peptides and Proteins
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