Trichogin GA IV: an antibacterial and protease-resistant peptide (Articolo in rivista)

Type
Label
  • Trichogin GA IV: an antibacterial and protease-resistant peptide (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/psc.1135 (literal)
Alternative label
  • Marta De Zotti; Barbara Biondi; Fernando Formaggio; Claudio Toniolo; Lorenzo Stella; Yoonkyung Park; Kyung-Soo Hahm (2009)
    Trichogin GA IV: an antibacterial and protease-resistant peptide
    in Journal of peptide science (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Marta De Zotti; Barbara Biondi; Fernando Formaggio; Claudio Toniolo; Lorenzo Stella; Yoonkyung Park; Kyung-Soo Hahm (literal)
Pagina inizio
  • 615 (literal)
Pagina fine
  • 619 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Selected and revised paper Conference: 1st Italy-Korea Symposium on Antimicrobial Peptides, Location: Chosun Univ, Gwangju, SOUTH KOREA, 24-25 July 2008. (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 15 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 9 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biomolecular Chemistry, Padova Unit, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy; Department of Chemical Sciences and Technologies, University of Rome ''Tor Vergata'', 00133 Rome, Italy; Department of Biotechnology, School of Natural Sciences, Chosun University, 501-759 Gwangju, Korea; Department of Bio-Materials, Research Center for Proteineous Materials, Chosun University, 501-759 Gwangju, Korea Department of Cellular and Molecular Medicine, College of Medicine, Chosun University, 501-759 Gwangju, Korea (literal)
Titolo
  • Trichogin GA IV: an antibacterial and protease-resistant peptide (literal)
Abstract
  • The antibacterial and hemolytic activities of the amphiphilic helical, membrane-active, lipopeptaibol trichogin GA IV and its [Leu(11)-OMe] analogue were compared to those of the partially helical or non-helical 8-meric or 4-meric, C-terminal short sequences, respectively. The study on trichogin GA IV was extended to several methicillin-resistant Stophylococcus aureus strains. Using a large set of enzymes, we also evaluated the resistance to proteolysis of all of the four peptides. (literal)
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