Computational studies on the backbone-dependent side-chain orientation induced by the (S,S)-CXC motif
| dc.contributor.author | Stavrakoudis, A. | en |
| dc.contributor.author | Tsikaris, V. | en |
| dc.date.accessioned | 2015-11-24T16:54:30Z | |
| dc.date.available | 2015-11-24T16:54:30Z | |
| dc.identifier.issn | 1075-2617 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10162 | |
| dc.rights | Default Licence | - |
| dc.subject | computational alanine scanning | en |
| dc.subject | backbone-dependent orientation | en |
| dc.subject | charge-charge interaction | en |
| dc.subject | computer simulation | en |
| dc.subject | cyclic peptides | en |
| dc.subject | disulfide cyclization | en |
| dc.subject | molecular dynamics | en |
| dc.subject | side-chain conformation | en |
| dc.subject | opioid receptor pharmacophore | en |
| dc.subject | tetrapeptide tyr-c<d-cys-phe-d-pen>oh jom-13 | en |
| dc.subject | molecular-dynamics simulations | en |
| dc.subject | cyclic-peptides | en |
| dc.subject | active-site | en |
| dc.subject | cxxc motif | en |
| dc.subject | model | en |
| dc.subject | tool | en |
| dc.subject | replacements | en |
| dc.subject | prediction | en |
| dc.title | Computational studies on the backbone-dependent side-chain orientation induced by the (S,S)-CXC motif | en |
| heal.abstract | Disulfide cyclization is a well-known procedure to impose conformational restriction to peptides undergoing backbone flexibility. Rigid conformations are induced only for small rings with a specific combination of amino acids. In this work. we present: a computational search of the backbone and backbone-dependent side-chain orientation of two series of linear and cyclic peptide analogs. The -C[XY]C- scaffold (where X,Y is arginine, aspartic acid or alanine residue) in Its open and (S,S) cyclic form was used for the design of the studied analogs Thidy-six compounds, resulting from the extension with one residue at either the N- or the C-termius were studied with classical MD. The local backbone conformation and the relative orientation of the X and Y side chains induced by either cyclization and/or the presence of file charged residues are discussed. From the present. study it is concluded that cyclization has a great impact on the synplanar orientation of the X and Y side chains in the (S,S)Ac-XCYC-NH(2) series of compounds while charge-charge Interaction has only a weak synergic effect. On the contrary, the antiplanar orientation is favored in the case of (S,S)Ac-CXCY-NH(2). Copyright (c) 2008 European Peptide Society and John Wiley & Sons, Ltd. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | Doi 10.1002/Psc.1066 | - |
| heal.identifier.secondary | <Go to ISI>://000262016400005 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1002/psc.1066/asset/1066_ftp.pdf?v=1&t=h0f8tfto&s=72b36695721c4cf92ed203299dcec581a2780a66 | - |
| heal.journalName | Journal of Peptide Science | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2008 | - |
| 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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