Design and synthesis of cationic Aib-containing antimicrobial peptides: conformational and biological studies

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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.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.accesscampus-
heal.fullTextAvailabilityTRUE-
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.journalNameJournal of Peptide Scienceen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2007-
heal.publisherWiley-Blackwellen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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