Antimicrobial and conformational studies of the active and inactive analogues of the protegrin‐1 peptide

@article{RodziewiczMotowido2010AntimicrobialAC,
  title={Antimicrobial and conformational studies of the active and inactive analogues of the protegrin‐1 peptide},
  author={S. Rodziewicz-Motowidło and B. Mickiewicz and K. Greber and E. Sikorska and Łukasz Szultka and E. Kamysz and W. Kamysz},
  journal={The FEBS Journal},
  year={2010},
  volume={277}
}
  • S. Rodziewicz-Motowidło, B. Mickiewicz, +4 authors W. Kamysz
  • Published 2010
  • Chemistry, Medicine
  • The FEBS Journal
  • The natural antimicrobial cationic peptide protegrin‐1 displays a broad spectrum of antimicrobial activity and rapidly kills pathogens by interacting with their cell membrane. We investigated the structure–activity relationships of three protegrin‐1 analogues: IB‐367 (RGGLCYCRGRFCVCVGR‐NH2), BM‐1 (RGLCYCRGRFCVCVG‐NH2) and BM‐2 (RGLCYRPRFVCVG‐NH2). Our antimicrobial and antifungal activity studies of these peptides showed that BM‐1 was much more active than IB‐367 against Gram‐positive bacteria… CONTINUE READING
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