Status: Bibliographieeintrag
Standort: ---
Exemplare:
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| Online-Ressource |
Verfasst von: | Nitsche, Christoph [VerfasserIn]  |
| Behnam, Mira A. M. [VerfasserIn]  |
| Steuer, Christian [VerfasserIn]  |
| Klein, Christian D. [VerfasserIn]  |
Titel: | Retro peptide-hybrids as selective inhibitors of the Dengue virus NS2B-NS3 protease |
Verf.angabe: | Christoph Nitsche, Mira A.M. Behnam, Christian Steuer, Christian D. Klein |
E-Jahr: | 2012 |
Jahr: | 26 February 2012 |
Umfang: | 8 S. |
Fussnoten: | Gesehen am 11.06.2018 |
Titel Quelle: | Enthalten in: Antiviral research |
Ort Quelle: | Amsterdam [u.a.] : Elsevier Science, 1981 |
Jahr Quelle: | 2012 |
Band/Heft Quelle: | 94(2012), 1, Seite 72-79 |
ISSN Quelle: | 1872-9096 |
Abstract: | New chemotherapeutics against Dengue virus and related flaviviruses are of growing interest in antiviral drug discovery. The viral serine protease NS2B-NS3 is a promising target for the development of such agents. Drug-like inhibitors of this protease with high affinity to the target are not available at the moment. The present work describes the discovery of new retro di- and tripeptide hybrids that do not necessarily require an electrophilic “warhead” to achieve affinities in the low micromolar range. The most active sequence in this series is the tripeptide R-Arg-Lys-Nle-NH2. By variation of the N-terminal groups (R) it could be shown that the previously described arylcyanoacrylamide moiety is a preferable group in this position. Retro tripeptide hybrids were found to be more active and more selective than retro dipeptide hybrids. A significant selectivity towards the Dengue virus protease could be shown in a counterscreen with thrombin and the West Nile virus protease. Alternative sequences to R-Arg-Lys-Nle-NH2 did not have higher affinities towards the Dengue virus protease, similar to retro-inverse sequences with d-lysine and d-arginine residues. The results of a competition assay with the known inhibitor aprotinin indicate that the N-terminal arylcyanoacrylamide residue of this compound class binds near the catalytic center of the enzyme. |
DOI: | doi:10.1016/j.antiviral.2012.02.008 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: http://dx.doi.org/10.1016/j.antiviral.2012.02.008 |
| Volltext: http://www.sciencedirect.com/science/article/pii/S0166354212000411 |
| DOI: https://doi.org/10.1016/j.antiviral.2012.02.008 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | Dengue virus |
| Hybrid retro peptides |
| NS2B-NS3 protease |
| Thrombin |
| West Nile virus |
K10plus-PPN: | 1576212165 |
Verknüpfungen: | → Zeitschrift |
Retro peptide-hybrids as selective inhibitors of the Dengue virus NS2B-NS3 protease / Nitsche, Christoph [VerfasserIn]; 26 February 2012 (Online-Ressource)
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