An NMR Study on the Phase Changes of Lipid Bilayers by Antimicrobial Peptides

Journal of the Korean Chemical Society

Chul Kim¹ 

关键词: 6°¢Çü ´Ü¸é ¸·´ë±¸Á¶ »ó;    Antimicrobial peptide;    Magainin 2;    Aurein 3.3;    Toroidal pore;    Hexagonal phase;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

The phase changes of 1-palmitoyl-d31-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC_d31) bilayers distorted by an antimicrobial peptide, a magainin 2 or an aurein 3.3 were investigated by using 2H solid-state NMR (SSNMR) spectroscopy. From the theoretical simulation of the experimental 2H solid-state NMR spectra the geometric structure constants and the lateral diffusion coefficients were obtained in the peptide-lipid mixture phases. Within five days of the peptide action on the lipid bilayers only the distorted alignment of the bilayers were measured but after 100 days an elliptic toroidal pore structure and an inverted hexagonal phase were formed in the presence of magainin 2 and aurein 3.3, respectively. In order to investigate the effect of an anionic lipid molecule on the actions of two peptides on the lipid bilayer, the same experiments were performed on the POPC_d31/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylglycerol (POPG) bilayer and the significant differences in the actions of two peptides on two bilayers of POPC_d31 and POPC_d31/POPG were measured.

【 授权许可】

Unknown