Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/10300
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dc.contributor.authorZikou, S.en
dc.contributor.authorKoukkou, A. I.en
dc.contributor.authorMastora, P.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorDrainas, C.en
dc.contributor.authorPanou-Pomonis, E.en
dc.date.accessioned2015-11-24T16:55:23Z-
dc.date.available2015-11-24T16:55:23Z-
dc.identifier.issn1075-2617-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10300-
dc.rightsDefault Licence-
dc.subjectcationic aib-containing peptidesen
dc.subjectantimicrobial activityen
dc.subjectproteolytic stabilityen
dc.subjecthemolytic assayen
dc.subjectcircular dichroismen
dc.subjectalpha-aminoisobutyric-aciden
dc.subjecttachyplesin-ien
dc.subjectmembranesen
dc.subjectrichen
dc.subjectantibioticsen
dc.titleDesign and synthesis of cationic Aib-containing antimicrobial peptides: conformational and biological studiesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1002/Psc.876-
heal.identifier.secondary<Go to ISI>://000248164400008-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/psc.876/asset/876_ftp.pdf?v=1&t=hmsy9zgm&s=6f216e46ef55ac6a3a7d55c2906434eb21d088b4-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2007-
heal.abstractDevelopment of antimicrobial peptides has attracted considerable attention in recent years due to the excessive use of antibiotics, which has led to multiresislant bacteria. Cationic amphiphilic Alb-containing peptide models Ac-(Aib-ArgAib-Leu)(n)-NH2, n = 1-4, and sequential cationic polypeptides (Arg-X-Gly)(n), X = Ala, Val, Leu, were prepared and studied for their antimicrobial and hemolytic activity, as well as for their proteolytic stability. Ac-(Aib-Arg-Aib-Leu)(n)-NH2, n = 2, 3 and the polypeptide (Arg-Leu-Gly)(n) exhibited significant antimicrobial activity, and they were nontoxic at their MIC values and resistant, in particular the Aib-peptide models, to enzymatic degradation. The conformational characteristics of the peptide models were studied by circular dichroism (CD). Structure-activity relationship studies revealed the importance of the amphipathic a-helical conformation of the reported peptides in inducing antimicrobial effects. It is concluded that peptide models comprising cationic amino acids (Arg), helicogenic and noncoding residues (Aib) and/or hydrophobic and helix-promoting components (Leu) may lead to the development of antimicrobial therapeutics. Copyright (C) 2007 European Peptide Society and John Wiley & Sons, Ltd.en
heal.publisherWiley-Blackwellen
heal.journalNameJournal of Peptide Scienceen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

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