Interaction of amphipathic peptides mediated by elastic membrane deformations

被引:5
作者
Akimov S.A. [1 ,2 ]
Aleksandrova V.V. [2 ]
Galimzyanov T.R. [1 ,2 ]
Bashkirov P.V. [1 ,3 ]
Batishchev O.V. [1 ]
机构
[1] Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, Leninskii pr. 31, build. 5, Moscow
[2] National University of Science and Technology MISiS, Leninskii pr. 4, Moscow
[3] Federal Research and Clinical Center of Physical-Chemical Medicine, ul. Malaya Pirogovskaya 1a, Moscow
基金
俄罗斯科学基金会;
关键词
amphipathic peptide; antimicrobial peptide; elasticity theory; lipid membrane; pore;
D O I
10.1134/S1990747817030035
中图分类号
学科分类号
摘要
Amphipathic alpha-helical peptides are perspective antimicrobial drugs. These peptides are partially embedded into the membrane to a shallow depth so that the longitudinal axis of the helix is parallel to the plane of the membrane or deviates from it by a small angle. In the framework of theory of elasticity of liquid crystals, adapted to lipid membranes, we calculated the energy of deformations occurring near the peptides partially embedded into the membrane. The energy of deformations is minimal when two peptides are parallel to each other and stay at a distance of about 5 nm. This configuration is stable with respect to small parallel displacements of the peptides and with respect to small variation of the angle between their axes both in the plane of the membrane and in the perpendicular direction. As a result of deformation the average thickness of the membrane decreases. The distribution of the elastic energy density has a maximum in the middle between the peptides. This region is the most likely place for formation of the through pores in the membrane. Since the equilibrium distance between the peptides is relatively large, it is assumed that the originally appearing pore should be purely lipidic. © 2017, Pleiades Publishing, Ltd.
引用
收藏
页码:206 / 216
页数:10
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