Publication details for Dr John M. SandersonDods, RH, Mosely, JA & Sanderson, JM (2012). The innate reactivity of a membrane associated peptide towards lipids: acyl transfer to melittin without enzyme catalysis. Organic & Biomolecular Chemistry 10(28): 5371-5378.
- Publication type: Journal Article
- ISSN/ISBN: 1477-0520 (print), 1477-0539 (electronic)
- DOI: 10.1039/c2ob07113d
- Further publication details on publisher web site
- Durham Research Online (DRO) - may include full text
Author(s) from Durham
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.