A synthetic 13-residue peptide corresponding to the hydrophobic region of bovine seminalplasmin has antibacterial activity and also causes lysis of red blood cells.

N Sitaram,R Nagaraj

doi:10.1016/s0021-9258(18)86965-4

Abstract

Seminalplasmin (SPLN), a 47-residue peptide present in bovine seminal plasma, is one of the few proteins isolated from mammalian sources having potent antibacterial activity. SPLN also interacts with sperm acrosomal and plasma membranes. On the basis of analysis of the primary structure of SPLN with respect to its relative hydrophobicity and hydrophilicity, a region comprising of 13-amino acids, Pro-Lys-Leu-Leu-Glu-Thr-Phe-Leu-Ser-Lys-Trp-Ile-Gly, has been delineated. It is demonstrated that a synthetic peptide corresponding to this 13-residue region inhibits growth of Escherichia coli like SPLN and also has the ability to lyse red blood cells.

Highlights

A Synthetic 13-Residue Peptide Corresponding to the Hydrophobic Region of Bovine Seminalplasmin Has Antibacterial Activity and Causes Lysis of Red Blood Cells*
Seminalplasmin (SPLN), a 47-residue peptide present in bovine seminal plasma, is one of the few proteins isolated from mammalian sources having potent antibacterial activity
Seminalplasmin (SPLN),’ a 47-residue peptide, present in bovine seminal plasma [7], is one of the few proteins isolated from mammalian sources, having potent antibacterial activity

Summary

Introduction

A Synthetic 13-Residue Peptide Corresponding to the Hydrophobic Region of Bovine Seminalplasmin Has Antibacterial Activity and Causes Lysis of Red Blood Cells*. On the basis of analysis of the primary structure of SPLN with respect to its relative hydrophobicity and hydrophilicity, a region comprising of 13-amino acids, Pro-Lys-Leu-Leu-Glu-. A large number of peptides comprising approximately 1540 residues, isolated from diverse sources such as insect venom [1, 2] and insect hemolymph [3] have potent antibacterial activity Many of these peptides exhibit lytic activity against eukaryotic cells [1, 4, 5]. The amino acid sequence of these peptides are such that the helix is amphiphilic in nature These peptides have charged residues either flanking the amphiphilic region or present in the helical sequence.

Methods

Results

Conclusion