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Identification of a second membrane‐active 13‐residue peptide segment in the antimicrobial protein, bovine seminalplasmin
Author(s) -
Sitaram N.,
Subbalakshmi C.,
Nagaraj R.
Publication year - 1993
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 - 10.1016/0014-5793(93)80935-n
Subject(s) - antibacterial activity , peptide , chemistry , residue (chemistry) , antimicrobial , vesicle , biochemistry , membrane protein , membrane , antimicrobial peptides , chromatography , bacteria , biology , organic chemistry , genetics
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.