Cookies

We use cookies to ensure that we give you the best experience on our website. By continuing to browse this repository, you give consent for essential cookies to be used. You can read more about our Privacy and Cookie Policy.


Durham Research Online
You are in:

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

Dods, R.H. and Mosely, J.A. and Sanderson, J.M. (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.

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.

Item Type:Article
Full text:(AM) Accepted Manuscript
Download PDF
(5325Kb)
Status:Peer-reviewed
Publisher Web site:http://dx.doi.org/10.1039/c2ob07113d
Date accepted:No date available
Date deposited:30 April 2013
Date of first online publication:July 2012
Date first made open access:No date available

Save or Share this output

Export:
Export
Look up in GoogleScholar