Structural and charge requirements for antimicrobial and hemolytic activity in the peptide PKLLETFLSKWIG, corresponding to the hydrophobic region of the antimicrobial protein bovine seminalplasmin

Sitaram, Narasimhaiah ; Subbalakshmi, Chilukcuri ; Nagaraj, Ramakrishnan (1995) Structural and charge requirements for antimicrobial and hemolytic activity in the peptide PKLLETFLSKWIG, corresponding to the hydrophobic region of the antimicrobial protein bovine seminalplasmin International Journal of Peptide and Protein Research, 46 (2). pp. 166-173. ISSN 0367-8377

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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1399-...

Related URL: http://dx.doi.org/10.1111/j.1399-3011.1995.tb01332.x

Abstract

Several analogs of the 13-residue antimicrobial and hemolytic peptide PKLLETFLSKWIG (SPF), which is the most hydrophobic region of the 47-residue antimicrobial protein seminalplasmin [Sitaram, N. & Nagaraj, R. (1990) J. Biol. Chem. 265, 10438-104423 have been synthesized. The antimicrobial and hemolytic properties of the peptides were investigated with a view to gain an insight into the structural and charge requirements for these activities of SPF. Peptides in which E was replaced by K exhibited considerably improved antimicrobial activity with no concomitant increase in hemolytic activity. A peptide in which the aromatic amino acids were replaced by leucine exhibited antimicrobial activity like those of the peptides which had aromatic amino acids. Interchange in the positions of E and K and total replacement of K by E resulted in complete loss of activity. The peptides having antimicrobial activities showed appreciable helical content in a hydrophobic environment, whereas inactive peptides did not. Thus, by suitable 'engineering' the biological activity of a short 13-residue peptide can be altered to yield peptides specifically having only antimicrobial activity with increased potency.

Item Type:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
Keywords:Antimicrobial Activity; Helical Conformation; Hemolysis; Peptide Engineering; Synthetic Peptides
ID Code:23977
Deposited On:01 Dec 2010 12:49
Last Modified:05 Mar 2011 05:27

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