Apolipoprotein A-I peptide models as probes to formulate potential inhibitors of the low-density lipoprotein oxidation
| dc.contributor.author | Darvari, M. I. | en |
| dc.contributor.author | Petraki, M. P. | en |
| dc.contributor.author | Tellis, C. | en |
| dc.contributor.author | Harilogis, K. | en |
| dc.contributor.author | Tselepis, A. D. | en |
| dc.contributor.author | Sakarellos-Daitsiotis, M. | en |
| dc.date.accessioned | 2015-11-24T16:52:27Z | |
| dc.date.available | 2015-11-24T16:52:27Z | |
| dc.identifier.issn | 1075-2617 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9887 | |
| dc.rights | Default Licence | - |
| dc.subject | apolipoprotein a-i helical peptide models | en |
| dc.subject | inhibitors of the ldl oxidation | en |
| dc.subject | hdl | en |
| dc.subject | cd of apoa-i helices | en |
| dc.subject | lipid-free | en |
| dc.subject | paf-acetylhydrolase | en |
| dc.subject | secondary structure | en |
| dc.subject | circular-dichroism | en |
| dc.subject | cholesterol efflux | en |
| dc.subject | amphipathic helix | en |
| dc.subject | crystal-structure | en |
| dc.subject | apoa-i | en |
| dc.subject | conformation | en |
| dc.subject | identification | en |
| dc.title | Apolipoprotein A-I peptide models as probes to formulate potential inhibitors of the low-density lipoprotein oxidation | en |
| heal.abstract | Apolipoprotein A-I (apoA-I), which constitutes the principal protein component of high-density lipoprotein, is responsible for its major antiatherogenic functions. Aiming at contributing to the development of potent inhibitors of low-density lipoprotein (LDL) peptide models of helices 4,6 and 9,10 of apoA-I were designed and synthesized. Specific amino acid substitutions, resulting in transformation of the original helix class A and Y to G according to the Schiffer and Edmundson helical wheel representation, were introduced in order to validate the contribution of these modifications in the inhibitory activity of the synthesized peptide models against the LDL oxidation. The role of Met at positions 112 (helix 4) and 148 (helix 6) as oxidant scavenger was also investigated. The helical characteristics of all the peptide models were studied by CD in membrane-mimicking microenvironments and compared with the original helices. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | Doi 10.1002/Psc.1391 | - |
| heal.identifier.secondary | <Go to ISI>://000296493600002 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/psc.1391/asset/psc1391.pdf?v=1&t=h0f7s087&s=27d11b1c063c7dea64ecc5c54823a26bd6dd3363 | - |
| heal.journalName | Journal of Peptide Science | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2011 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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