Probing the lipid-protein interface using model transmembrane peptides with a covalently linked acyl chain.

ABSTRACT: The aim of this study was to gain insight into how interactions between proteins and lipids in membranes are sensed at the protein-lipid interface. As a probe to analyze this interface, we used deuterium-labeled acyl chains that were covalently linked to a model transmembrane peptide. First, a perdeuterated palmitoyl chain was coupled to the Trp-flanked peptide WALP23 (Ac-CGWW(LA)(8)LWWA-NH(2)), and the deuterium NMR spectrum was analyzed in di-C18:1-phosphatidylcholine (PC) bilayers. We found that the chain order of this peptide-linked chain is rather similar to that of a noncovalently coupled perdeuterated palmitoyl chain, except that it exhibits a slightly lower order. Similar results were obtained when site-specific deuterium labels were used and when the palmitoyl chain was attached t

SUBMITTER: Nyholm TK 

PROVIDER: S-EPMC3192971 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature