The Influence of Lipid Bilayer Physicochemical Properties on Gramicidin A Conformer Preferences.

ABSTRACT: The conformational preferences adopted by gramicidin A (GA) dimers inserted into phospholipid bilayers are reported as a function of the bilayer cholesterol content, temperature, and incubation time. Through use of vesicle capture-freeze drying methodology, GA dimers were captured in lipid bilayers and the conformational preferences of the complex were analyzed using ion mobility-mass spectrometry. Perturbations that affect the physicochemical interactions in the lipid bilayer such as cholesterol incorporation, temperature, and incubation time directly alter the conformer preferences of the complex. Regardless of bilayer cholesterol concentration, the antiparallel double helix (ADH) conformation was observed to be most abundant for GA dimers in bilayers composed of lipids with 12 to 22 car

SUBMITTER: Patrick JW 

PROVIDER: S-EPMC4850349 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature