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

Dods, RH; Mosely, JA; Sanderson, JM

doi:10.1039/c2ob07113d

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

Dods, RH; Mosely, JA; Sanderson, JM

Authors

RH Dods

JA Mosely

Dr John Sanderson j.m.sanderson@durham.ac.uk
Associate Professor

Abstract

The innate reactivity of the peptide melittin (H-GIGAVLKVLTTGLPALISWIKRKRQQ-NH2) towards membrane lipids has been explored using LC-MS methods. The high sensitivity afforded by LC-MS analysis enabled acyl transfer to the peptide to be detected, within 4 h, from membranes composed of phosphocholines (PCs). Acyl transfer from PCs was also observed from mixtures of PC with phosphoserine (PS) or phosphoglycerol (PG). In the latter case, transfer from PG was also detected. The half-lives for melittin conversion varied between 24 h and 75 h, being fastest for POPC and slowest for DOPC/DMPG mixtures. The order of reactivity for amino groups on the peptide was N-terminus > K23 ≫ K21 > K7. Products arising from double-acylation of melittin were detected as minor components, together with a putative component derived from transesterification involving S18 of the peptide.

Citation

Dods, R., Mosely, J., & Sanderson, J. (2012). The innate reactivity of a membrane associated peptide towards lipids: acyl transfer to melittin without enzyme catalysis. Organic and Biomolecular Chemistry, 10(28), 5371-5378. https://doi.org/10.1039/c2ob07113d

Journal Article Type	Article
Publication Date	Jul 1, 2012
Deposit Date	Apr 4, 2012
Publicly Available Date	Apr 30, 2013
Journal	Organic and Biomolecular Chemistry
Print ISSN	1477-0520
Electronic ISSN	1477-0539
Publisher	Royal Society of Chemistry
Peer Reviewed	Peer Reviewed
Volume	10
Issue	28
Pages	5371-5378
DOI	https://doi.org/10.1039/c2ob07113d