Comparative molecular dynamics study of the structural properties of melittin in water and trifluoroethanol/water

被引：0

作者：

Naumenkova T.V. ^{[1
]}

Levtsova O.V. ^{[1
]}

Nikolaev I.N. ^{[2
]}

Shaitan K.V. ^{[1
]}

机构：

[1] Moscow State University, Vorob'evy Gory, Moscow

[2] Yakutsk State University, Yakutsk

来源：

Biophysics | 2010年 / 55卷 / 1期

关键词：

2,2,2-trifluoroethanol; Antimicrobial peptide; Melittin; Molecular dynamics; Secondary structure;

D O I：

10.1134/S0006350910010057

中图分类号：

学科分类号：

摘要：

The structural properties and dynamic behavior of the antimicrobial peptide melittin in hydrophobic and polar environments have been investigated. The main characteristics of the secondary structure of melittin in different media have been analyzed and compared with the data on an ideal α-helix. It has been shown that melittin is an α-helix bent in the region of Pro14; the N-terminus of the peptide tends to unfold, while the C-terminal segment (residues 14-23) retains a helical structure for 20 ns of the simulation. 2,2,2-Trifluoroethanol molecules stabilize the helical structure of the peptide by lowering the dielectric constant of the environment and preferentially accumulating near particular sites of the polypeptide chain. © 2010 Pleiades Publishing, Ltd.

引用

页码：24 / 28

页数：4

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