Effect of disulphide bond position on salt resistance and LPS-neutralizing activity of α-helical homo-dimeric model antimicrobial peptides

BMB Reports

Yong Hai Nan^1¹  Song Yub Shin^1,2² 

[1] Department of Bio-Materials, Graduate School^1;Department of Cellular &^2;Molecular Medicine, School of Medicine, Chosun University, Gwangju 501-759, Korea^3

关键词: Antimicrobial peptide;   

DOI  :  

学科分类：生物化学/生物物理

来源: Korean Society for Biochemistry and Molecular Biology

【 摘 要 】

To investigate the effects of disulphide bond position on the salt resistance and lipopolysaccharide (LPS)-neutralizing activity of α-helical homo-dimeric antimicrobial peptides (AMPs), we synthesized an α-helical model peptide (K6L4W1) and its homo-dimeric peptides (di-K(6)L(4)W(1)-N, di-K(6)L(4)W(1)-M, and di-K(6)L(4)W(1)-C) with a disulphide bond at the N-terminus, the central position, and the C-terminus of the molecules, respectively. Unlike (6)L(4)W(1) and di-K(6)L(4)W(1)-M, the antimicrobial activity of di-K(6)L(4)W(1)-N and di-K(6)L(4)W(1)-C was unaffected by 150 mM NaCl. Both di-K(6)L(4)W(1)-N and di-K(6)L(4)W(1)-C caused much greater inhibitory effects on nitric oxide (NO) release in LPS-induced mouse macrophage RAW 264.7 cells, compared to di-K(6)L(4)W(1)-M. Taken together, our results indicate that the presence of a disulphide bond at the N- or C-terminus of the molecule, rather than at the central position, is more effective when designing salt-resistant α-helical homo-dimeric AMPs with potent antimicrobial and LPS-neutralizing activities.

【 授权许可】

Unknown