Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P.

@article{Kazazic2002MutationalAO,
  title={Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P.},
  author={Maja Kazazic and Jon Nissen-Meyer and Gunnar Fimland},
  journal={Microbiology},
  year={2002},
  volume={148 Pt 7},
  pages={2019-27}
}
The significance of charged residues for the target-cell binding, potency and specificity of pediocin-like bacteriocins has been studied by site-directed mutagenesis of sakacin P. Most of the charged residues are located in the N-terminal half, which is thought to mediate the initial binding of these bacteriocins to target cells through electrostatic interaction. All the mutated peptides in which the net positive charge was reduced by one (by replacing a charged residue with threonine… CONTINUE READING

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Unmodified peptide-bacteriocins (class II) produced by lactic acid bacteria

  • P Role of charged residues in sakacin
  • Peptide Antibiotics : Discovery, Modes of Action…
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