Biological activities of C‐terminal 15‐residue synthetic fragment of melittin: design of an analog with improved antibacterial activity

FEBS Letters

Subbalakshmi, C.¹  Sitaram, N.¹  Nagaraj, R.¹ 

[1] Centre for Cellular and Molecular Biology, Uppal road, Hyderabad 500 007, India

关键词: Melittin;    C-terminal synthetic peptide;    Analog with improved activity;    Antibacterial activity;    Hemolytic activity;    Folding;    Aggregation;   

DOI  :  10.1016/S0014-5793(99)00328-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Melittin, the 26-residue predominant toxic peptide from bee venom, exhibits potent antibacterial activity in addition to its hemolytic activity. The synthetic peptide of 15 residues corresponding to its C-terminal end (MCF), which encompasses its most amphiphilic segment, is now being shown to possess antibacterial activity about 5–7 times less compared to that of melittin. MCF, however, is 300 times less hemolytic. An analog of MCF, MCFA, in which two cationic residues have been trans-positioned to the N-terminal region from the C-terminal region, exhibits antibacterial activity comparable to that of melittin, but is only marginally more hemolytic than MCF. The biophysical properties of the peptides, like folding and aggregation, correlate well with their biological properties.

【 授权许可】

Unknown