Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

FEBS Letters

Subbalakshmi, Chilukuri¹  Sitaram, Narasimhaiah¹  Nagaraj, Ramakrishnan¹  Krishnakumari, Viswanath¹ 

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

关键词: Antimicrobial protein;    Antimicrobial peptide;    27-residue peptide;    Hemolytic activity;    Secondary structure;    Seminalplasmin/caltrin;   

DOI  :  10.1016/S0014-5793(96)01406-8

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 isolated from bovine seminal plasma having potent antimicrobial activity against a broad spectrum of microorganisms. SPLN, also known as caltrin, acts as a calcium transport regulator in bovine sperms. Analysis of the sequence of SPLN reveals a 27-residue stretch with the sequence SLSRYAKLANRLANPKLLETFLSKWIG more hydrophobic than the rest of the protein. It is demonstrated that a synthetic peptide corresponding to this 27-residue segment has antimicrobial activity comparable to that of SPLN. It does not exhibit hemolytic activity at concentrations where antibacterial activity is observed. Since P27 can be conveniently obtained in large amounts by chemical synthesis, it could serve not only as a starting compound to obtain peptides with improved antibacterial activity but also to understand the role of SPLN in reproductive physiology.

【 授权许可】

Unknown