Five disulfide bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.).

@article{Bergh2002FiveDB,
  title={Five disulfide bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.).},
  author={Karolien P B Van den Bergh and Paul Proost and Jo Van Damme and Jozef Coosemans and Els J. M. van Damme and Willy J. Peumans},
  journal={FEBS letters},
  year={2002},
  volume={530 1-3},
  pages={181-5}
}
A small 45 amino acid residue antifungal polypeptide was isolated from the bark of spindle tree (Euonymus europaeus L.). Though the primary structure of this so-called E. europaeus chitin-binding protein or Ee-CBP is highly similar to the hevein domain, it distinguishes itself from most previously identified hevein-type antimicrobial peptides (AMP) by the presence of two extra cysteine residues that form an extra disulfide bond. Due to these five disulfide bonds Ee-CBP is a remarkably stable… CONTINUE READING

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