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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Minchev, I. | en |
| dc.contributor.author | Vladimirova, S. | en |
| dc.contributor.author | Vezenkov, L. | en |
| dc.contributor.author | Bijev, A. | en |
| dc.contributor.author | Moussis, V. | en |
| dc.contributor.author | Nikolaeva-Glomb, L. | en |
| dc.contributor.author | Tsikaris, V. | en |
| dc.contributor.author | Czeuz, M. | en |
| dc.contributor.author | Galabov, A. | en |
| dc.date.accessioned | 2015-11-24T16:55:26Z | - |
| dc.date.available | 2015-11-24T16:55:26Z | - |
| dc.identifier.issn | 0929-8665 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10308 | - |
| dc.rights | Default Licence | - |
| dc.subject | antipicornaviral compounds | en |
| dc.subject | pyrroles | en |
| dc.subject | peptidomimetics | en |
| dc.subject | 3c inhibitors | en |
| dc.subject | coxsackievirus | en |
| dc.subject | spps | en |
| dc.subject | rhinovirus 3c protease | en |
| dc.subject | escherichia-coli | en |
| dc.subject | inhibitors | en |
| dc.subject | derivatives | en |
| dc.subject | poliovirus | en |
| dc.subject | cleavage | en |
| dc.title | Design, synthesis and biological evaluation of antipicornaviral pyrrole-containing peptidomimetics | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://000253577500013 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2007 | - |
| heal.abstract | A series of new peptidomimetics based on the tripeptide sequence Z-Leu-Phe-Gln-OH were synthesized, with ten of these including the nitrogen atom of the N-terminal amino acid incorporated into the pyrrole cycle. The synthesized compounds were tested for antiviral activity by agar-diffusion plaque inhibition test against Coxsackievirus B1 replication in FL cell. Four of the products were observed to possess an antiviral activity, which was proven to be significant for one product. N-terminal pyrrole moiety and C-terminal free carboxyl function are available in all active compounds. On the other hand, their corresponding -OBzl and -OBut esters are inactive. | en |
| heal.journalName | Protein Pept Lett | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
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