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Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin
Author(s) -
Sitaram Narasimhaiah,
Subbalakshmi Chilukuri,
Krishnakumari Viswanath,
Nagaraj Ramakrishnan
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01406-8
Subject(s) - residue (chemistry) , antimicrobial , antibacterial activity , chemistry , biochemistry , chromatography , biology , bacteria , organic chemistry , genetics
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.