The innate reactivity of a membrane associated peptide towards lipids: acyl transfer to melittin without enzyme catalysis

Abstract

. (2012) 'The innate reactivity of a membrane associated peptide towards lipids : acyl transfer to melittin without enzyme catalysis.', Organic biomolecular chemistry., 10 (28). pp. 5371-5378.Further information on publisher's website:Publisher's copyright statement:Additional information: Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details.

Acyl Transfer from Membrane Lipids to Peptides Is a Generic Process

“…Product assignment has been described elsewhere. 4 At the peptide concentrations used, detection of products by UV absorbance was not feasible, preventing precise determination of the degree of conversion of melittin to lipidated products. Using ion chromatograms, quantification of each species was not facile, in part because the concentration dependence of the ionisation efficiency for all species was uncharacterised, and in part because the elution of some products was overlapping, which would be expected to bias peak areas in favor 8 of the species with higher ionisation efficiency.…”

“…Recently, acyl group transfer from phospholipids to the peptide melittin was described. 3,4 This acyl transfer, termed intrinsic lipidation, did not require enzyme catalysis and therefore reflects an innate reactivity of the peptide towards lipids. This reactivity is of interest because it does not require reagents other than the lipid membrane and the peptide itself and is consequently a process to which all membrane-active peptides and proteins are potentially subject.…”

Resolving the kinetics of lipid, protein and peptide diffusion in membranes

“…Similar periods of hours were required for complete It has recently become evident that even in simple model peptide-lipid systems, the lipid cannot be considered as an inert medium in which peptide binding and reorientation (Pridmore et al, 2011). The same reaction has a t 1/2 of ≈24 h in bicarbonate buffer at pH 7.4, with acylation products detectable after 4 h (Dods et al, 2012). Acylation occurs primarily at the N-terminal amino group of melittin, as well as the amino groups of lysine side chains, most notably the lysine closest to the Cterminus of the peptide.…”

The lipidation profile of aquaporin-0 correlates with the acyl composition of phosphoethanolamine lipids in lens membranes

“…At this position, palmitoyl, oleoyl and stearoyl adducts of the 234-259 sequence are clearly resolved. Within this sequence, there is a single internal, highly conserved lysine (K238) [5] that, as expected [2], is not cleaved by trypsin when lipidated. The ion abundances of these acyl adducts are in the order oleoyl > palmitoyl > stearoyl.…”

“…The benchmark peptide for this process is melittin, which is lipidated in synthetic liposomes on the N-terminal amino group and on the side chains of internal lysine and, less commonly, serine residues [2,3]. In the intrinsic lipidation reactions of melittin, little selectivity is found for the aminolysis reaction with the sn-1 and sn-2 glyceryl esters, and the acyl group distribution of the lipidated products reflects the fatty acyl composition of the liposomal membrane.…”