Antimicrobial activity and conformation of Gaegurin-6 amide and its analogs

被引:13
|
作者
Lee, KH
Hong, SY
Oh, JE
Lee, BJ
Choi, BS
机构
[1] Mogam Biotechnol Res Inst, Prot Chem Lab, Kyunggi Do 449910, South Korea
[2] Seoul Natl Univ, Seoul 151742, South Korea
[3] Korea Adv Inst Sci & Technol, Taejon 305701, South Korea
关键词
antimicrobial peptide; circular dichroism; disulfide bridge; Rana; secondary structure;
D O I
10.1016/S0196-9781(98)00119-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A function of the intra-disulfide bridge located at the C-terminal of Rana peptides has not been extensively studied. To investigate the function of the disulfide bridge related to the activity and the structure, we chose Gaegurin-6, isolated from Rana rugosa as a model peptide and synthesized linear analogs. The reduction of the disulfide bridge resulted in the complete loss of antimicrobial activity while replacements of cysteines by serines retained antimicrobial activity. Circular dichroism spectra from a titration of the peptides in sodium dodecyl sulfate indicated that the disulfide bridge of Gaegurin-6 might stabilize the induction of an alpha helical structure in Lipid membranes and the alpha helical forming propensity of the peptides correlated with antimicrobial activity. (C) 1998 Elsevier Science Inc.
引用
收藏
页码:1653 / 1658
页数:6
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