J Pept Sci, 2016, 22(2):98-105

Effective lipid-detergent system for study of membrane active peptides in fluid liposomes

The structure of peptide antibiotic gramicidin A (gA) was studied in phosphatidylcholin liposomes modified by nonionic detergent Triton X-100. First, the detergent: lipid ratio at which the saturation of lipid membrane by Triton X-100 occurs (Resat), was determined by light scattering. Measurements of steady-state fluorescence anisotropy of 1,6-diphenyl-1,3,5-hexatriene at sublytic concentrations of detergent showed that after saturation of the membrane by Triton X-100 microviscosity of lipid bilayer is reduced by 20%. The equilibrium conformational state of gA in phosphatidylcholine liposomes at Resatwas studied by CD spectroscopy. It was found that the conformational state of this channel-forming peptide changed crucially when Triton X-100 induced transition to more fluid membranes. The gA single-channel measurements were made with Triton X-100 containing bilayers. Tentative assignment of the channel type and gA structures was made by correlation of CD data with conductance histograms. Lipid-detergent system with variable viscosity developed in this work can be used to study the structure and folding of other membrane-active peptides.

IBCH: 4039
Ссылка на статью в журнале: http://doi.wiley.com/10.1002/psc.2845
Кол-во цитирований на 03.2024: 2
Данные статьи проверены модераторами 2016-02-01

Список научных проектов, где отмечена публикация

  1. Белки и пептиды в постгеномную эру. Структурно-функциональные исследования для решения фундаментальных задач и направленного конструирования инновационных лекарственных средств (6 Января 2014 года — 31 Декабря 2018 года). Габибов А.Г.. Грант, РНФ.