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Synthetic analogs of anoplin show improved antimicrobial activities
Author(s) -
Munk Jens K.,
Uggerhøj Lars Erik,
Poulsen Tanja J.,
FrimodtMøller Niels,
Wimmer Reinhard,
Nyberg Nils T.,
Hansen Paul R.
Publication year - 2013
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2548
Subject(s) - antimicrobial , enterococcus faecium , candida albicans , staphylococcus aureus , chemistry , microbiology and biotechnology , pseudomonas aeruginosa , escherichia coli , peptide , enterococcus , bacteria , biochemistry , antibiotics , biology , genetics , gene
We present the antimicrobial and hemolytic activities of the decapeptide anoplin and 19 analogs thereof tested against methicillin‐resistant Staphylococcus aureus ATCC 33591 (MRSA), Escherichia coli (ATCC 25922), Pseudomonas aeruginosa (ATCC 27853), vancomycin‐resistant Enterococcus faecium (ATCC 700221) (VRE), and Candida albicans (ATCC 200955). The anoplin analogs contain substitutions in amino acid positions 2, 3, 5, 6, 8, 9, and 10. We use these peptides to study the effect of altering the charge and hydrophobicity of anoplin on activity against red blood cells and microorganisms. We find that increasing the charge and/or hydrophobicity improves antimicrobial activity and increases hemolytic activity. For each strain tested, we identify at least six anoplin analogs with an improved therapeutic index compared with anoplin, the only exception being Enterococcus faecium , against which only few compounds are more specific than anoplin. Both 2Nal 6 and Cha 6 show improved therapeutic index against all strains tested. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.