Identification of a second membrane‐active 13‐residue peptide segment in the antimicrobial protein, bovine seminalplasmin

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: Antimicrobial protein;    Antimicrobial peptide;    13-Residue peptide;    Bovine seminalplasmin;    Membrane activity;    Hemolytic activity;   

DOI  :  10.1016/0014-5793(93)80935-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Seminalplasmin (SPLN) is a 47-residue protein from bovine seminalplasma having broad-spectrum antibacterial activity. The protein has no hemolytic activity. SPLN interacts with lipid vesicles and its antibacterial activity appears to stem from its ability to permeabilize the bacterial plasma membrane. Analysis of SPLN's primary structure, with respect to its relative hydrophobicity and hydrophilicity, revealed a segment, PKLLETFLSKWIG, more hydrophobic than the rest of the protein. A synthetic peptide corresponding to this region had not only antibacterial activity but also hemolytic properties. Analysis of the SPLN sequence based on hydrophobic moment plots has revealed a second segment, SLSRYAKLANRLA, which could be membrane active. A synthetic peptide corresponding to this region shows only antibacterial activity with no hemolytic activity.

【 授权许可】

Unknown