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Wide-spectrum antibiotic activity of synthetic, amphipathic peptides

TIOZZO, ELKA
•
G. ROCCO
•
TOSSI, ALESSANDRO
•
ROMEO, DOMENICO
1998
  • journal article

Periodico
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Abstract
PGYa and PGAa are synthetic, amphipathic, α-helical peptides that were designed using a novel 'sequence template' approach. Their antimicrobial activity was tested against several pathogenic clinical isolates, most of which were multiply resistant to conventional antibiotics. PGYa appeared to be more active towards Gram-positive species (MIC = 0.5-4 μM), towards such Gram negative species as P. aeruginosa, X. maltophilia, E. coli, K. pneumoniae and S. enteritidis MIC = 1-4 μM), and towards the filamentous fungus A. niger (MIC = 8 μM). Conversely, PGAa showed the greater activity towards three Candida species (MIC = 2-16 μM). The peptides were shown to have a bactericidal activity, resulting in a decrease of viability for both Gram-positive and -negative bacteria of 3-6 logs within 60 min. Scanning electron microscopy of S. aureus and E. coli treated with PGYa shows considerable roughening and blebbing of the bacterial surfaces providing conclusive evidence that the peptide is membrane active.
DOI
10.1006/bbrc.1998.9114
WOS
WOS:000075363000038
Archivio
http://hdl.handle.net/11368/1708352
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0032504531
Diritti
metadata only access
Soggetti
  • cathelicidin

  • antimicrobial peptide...

  • amphipathic helix

  • model peptide

  • membrane permeabiliza...

Web of Science© citazioni
51
Data di acquisizione
Mar 23, 2024
Visualizzazioni
2
Data di acquisizione
Apr 19, 2024
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