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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Zikou, S. | en |
| dc.contributor.author | Koukkou, A. I. | en |
| dc.contributor.author | Mastora, P. | en |
| dc.contributor.author | Sakarellos-Daitsiotis, M. | en |
| dc.contributor.author | Sakarellos, C. | en |
| dc.contributor.author | Drainas, C. | en |
| dc.contributor.author | Panou-Pomonis, E. | en |
| dc.date.accessioned | 2015-11-24T16:55:23Z | - |
| dc.date.available | 2015-11-24T16:55:23Z | - |
| dc.identifier.issn | 1075-2617 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10300 | - |
| dc.rights | Default Licence | - |
| dc.subject | cationic aib-containing peptides | en |
| dc.subject | antimicrobial activity | en |
| dc.subject | proteolytic stability | en |
| dc.subject | hemolytic assay | en |
| dc.subject | circular dichroism | en |
| dc.subject | alpha-aminoisobutyric-acid | en |
| dc.subject | tachyplesin-i | en |
| dc.subject | membranes | en |
| dc.subject | rich | en |
| dc.subject | antibiotics | en |
| dc.title | Design and synthesis of cationic Aib-containing antimicrobial peptides: conformational and biological studies | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1002/Psc.876 | - |
| heal.identifier.secondary | <Go to ISI>://000248164400008 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/psc.876/asset/876_ftp.pdf?v=1&t=hmsy9zgm&s=6f216e46ef55ac6a3a7d55c2906434eb21d088b4 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2007 | - |
| heal.abstract | Development 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.publisher | Wiley-Blackwell | en |
| heal.journalName | Journal of Peptide Science | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Zikou-2007-Design and synthesis.pdf | 150.95 kB | Adobe PDF | View/Open Request a copy |
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