Improving specificity vs bacterial thymidylate synthases through N-dansyl modulation of didansyltyrosine.
Donatella Tondi, Alberto Venturelli, Stefania Ferrari, Stefano Ghelli, M Paola Costi
文献索引:J. Med. Chem. 48 , 913-916, (2005)
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摘要
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.
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