A synthetic 13-residue peptide corresponding to the hydrophobic region of bovine seminalplasmin has antibacterial activity and also 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. 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.
Sitaram
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N
Centre for Cellular and Molecular Biology, Hyderabad, India.
Nagaraj
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R
D000469:Alkaline Phosphatase / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000138:chemical synthesis*; D002417:Cattle; D002942:Circular Dichroism; D004912:Erythrocytes / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology; D006461:Hemolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000494:pharmacology; D011487:Protein Conformation; D011506:Proteins / Q000138:chemical synthesis* / Q000494:pharmacology; D051381:Rats; D029607:Seminal Vesicle Secretory Proteins; D001616:beta-Galactosidase / Q000378:metabolism
D000900:Anti-Bacterial Agents; D009842:Oligopeptides; D011506:Proteins; D029607:Seminal Vesicle Secretory Proteins; D000469:Alkaline Phosphatase; D001616:beta-Galactosidase