Interaction between heat shock proteins and antimicrobial peptides.

@article{Otvos2000InteractionBH,
  title={Interaction between heat shock proteins and antimicrobial peptides.},
  author={Laszlo Otvos and O Insug and M. Elizabeth Rogers and Patricia J. deAngelis Consolvo and Barry A. Condie and S{\'a}ndor Lovas and Philippe Bulet and Magdalena Blaszczyk-Thurin},
  journal={Biochemistry},
  year={2000},
  volume={39 46},
  pages={
          14150-9
        }
}
Drosocin, pyrrhocoricin, and apidaecin, representing the short (18-20 amino acid residues) proline-rich antibacterial peptide family, originally isolated from insects, were shown to act on a target bacterial protein in a stereospecific manner. Native pyrrhocoricin and one of its analogues designed for this purpose protect mice from bacterial challenge and, therefore, may represent alternatives to existing antimicrobial drugs. Furthermore, this mode of action can be a basis for the design of a… CONTINUE READING

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