Antimicrobial activity of Bac7 fragments against drug-resistant clinical isolates
Ten peptides from 13 to 35 residues in length and covering the whole sequence of the Pro-rich peptide Bac7 were synthesized to identify the domain responsible for its antimicrobial activity. At least 16 residues of the highly cationic N-terminal sequence were required to maintain the activity agains...
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Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2004-12, Vol.25 (12), p.2055-2061 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Ten peptides from 13 to 35 residues in length and covering the whole sequence of the Pro-rich peptide Bac7 were synthesized to identify the domain responsible for its antimicrobial activity. At least 16 residues of the highly cationic N-terminal sequence were required to maintain the activity against Gram-negative bacteria. The fragments Bac7(1–35) and, to a lesser extent, Bac7(1–16) proved active against a panel of antibiotic-resistant clinical isolates of Gram-negative bacteria, with the notable exception of
Burkholderia cepacia. In addition, when tested against fungi, the longer fragment was also active against collection strains and clinical isolates of
Cryptococcus neoformans, but not towards clinical isolates of
Candida albicans. |
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ISSN: | 0196-9781 1873-5169 |
DOI: | 10.1016/j.peptides.2004.08.004 |