Structure-activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin.

@article{Chan1996StructureactivityRI,
  title={Structure-activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin.},
  author={Weng C Chan and M L Leyland and Joshua J Clark and Helen M. Dodd and Lu Yun Lian and Michael J. Gasson and Barrie W. Bycroft and Gordon C. K. Roberts},
  journal={FEBS letters},
  year={1996},
  volume={390 2},
  pages={129-32}
}
The post-translationally modified peptide antibiotic nisin has been cleaved by a number of proteases and the fragments produced purified, characterised chemically, and assayed for activity in inhibiting the growth of Lactococcus lactis MG1614 and Micrococcus luteus NCDO8166. These results provide information on the importance of different parts of the nisin molecule for its growth-inhibition activity. Removal of the C-terminal five residues leads to approximately a 10-fold decrease in potency… CONTINUE READING

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Eds.) Nisin and Novel Lantibiotics

G. Jung, Sahl, H.-G
ESCOM Science, • 1991
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Nisin and Novel Lanti - biotics

H.-G. Sahl
1991

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K. Rayman, A. Hurst
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