N,O-Didansyl-L-tyrosine (DDT) represented the starting lead for further development of novel non-substrate-like inhibitors of bacterial thymidylate synthase. The N-dansyl structure modulation led to a submicromolar inhibitor of Lactobacillus casei TS (LcTS), which is highly specific with respect to human TS (hTS). Using molecular dynamics simulation, a binding mode for DDT vs LcTS was predicted, explaining activity and species-specificity along the series.
Improving specificity vs bacterial thymidylate synthases through N-dansyl modulation of didansyltyrosine / Tondi, Donatella; Venturelli, A.; Ferrari, Stefania; Ghelli, S.; Costi, Maria Paola. - In: JOURNAL OF MEDICINAL CHEMISTRY. - ISSN 0022-2623. - STAMPA. - 48:4(2005), pp. 913-916. [10.1021/jm0491445]
Improving specificity vs bacterial thymidylate synthases through N-dansyl modulation of didansyltyrosine
TONDI, Donatella;A. Venturelli;FERRARI, Stefania;COSTI, Maria Paola
2005
Abstract
N,O-Didansyl-L-tyrosine (DDT) represented the starting lead for further development of novel non-substrate-like inhibitors of bacterial thymidylate synthase. The N-dansyl structure modulation led to a submicromolar inhibitor of Lactobacillus casei TS (LcTS), which is highly specific with respect to human TS (hTS). Using molecular dynamics simulation, a binding mode for DDT vs LcTS was predicted, explaining activity and species-specificity along the series.
| File | Dimensione | Formato | |
|---|---|---|---|
|
JMC2005.pdf
Solo gestori archivio
Tipologia:
VOR - Versione pubblicata dall'editore
Dimensione
274.54 kB
Formato
Adobe PDF
|
274.54 kB | Adobe PDF | Visualizza/Apri Richiedi una copia |
Pubblicazioni consigliate
I metadati presenti in IRIS UNIMORE sono rilasciati con licenza Creative Commons CC0 1.0 Universal, mentre i file delle pubblicazioni sono rilasciati con licenza Attribuzione 4.0 Internazionale (CC BY 4.0), salvo diversa indicazione.
In caso di violazione di copyright, contattare Supporto Iris
