Change of glutamic acid to lysine in a 13-residue antibacterial and hemolytic peptide results in enhanced antibacterial activity without increase in hemolytic activity

N Sitaram; M Chandy; V N Pillai; R Nagaraj

doi:10.1128/AAC.36.11.2468

Change of glutamic acid to lysine in a 13-residue antibacterial and hemolytic peptide results in enhanced antibacterial activity without increase in hemolytic activity

Antimicrob Agents Chemother. 1992 Nov;36(11):2468-72. doi: 10.1128/AAC.36.11.2468.

Authors

N Sitaram¹, M Chandy, V N Pillai, R Nagaraj

Affiliation

¹ Centre for Cellular and Molecular Biology, Hyderabad, India.

Abstract

A 13-residue peptide corresponding to a hydrophobic segment of the antimicrobial 47-residue peptide seminalplasmin, PKLLETFLSKWIG (SPF), has been shown to have antibacterial and hemolytic activities (N. Sitaram and R. Nagaraj, J. Biol. Chem. 265:10438-10442, 1990). In an effort to get an insight into the structural and charge requirements for these biological activities, an analog of SPF in which Glu has been replaced with Lys has been synthesized and its antibacterial and hemolytic properties have been examined. It has been demonstrated that the analog, SPFK, exhibits potent antibacterial activity at concentrations at which hemolysis does not occur.

Publication types

Comparative Study

MeSH terms

Amino Acid Sequence
Animals
Anti-Bacterial Agents / chemistry
Anti-Bacterial Agents / pharmacology*
Erythrocytes / drug effects
Escherichia coli / drug effects
Glutamates / chemistry*
Glutamic Acid
Hemolysis / drug effects*
Hydrogen-Ion Concentration
Kinetics
Lysine / chemistry*
Membrane Potentials / drug effects
Molecular Sequence Data
Peptide Fragments / pharmacology
Peptides / pharmacology
Proteins / chemistry
Proteins / pharmacology*
Rats
Seminal Vesicle Secretory Proteins*
Structure-Activity Relationship

Substances

Anti-Bacterial Agents
Glutamates
Peptide Fragments
Peptides
Proteins
Seminal Vesicle Secretory Proteins
seminalplasmin, Lys(13)-
Glutamic Acid
Lysine