Improving specificity vs bacterial thymidylate synthases through N-dansyl modulation of didansyltyrosine.
作者信息
Tondi Donatella, Venturelli Alberto, Ferrari Stefania, Ghelli Stefano, Costi M Paola
机构信息
Dipartimento di Scienze Farmaceutiche, Università degli Studi di Modena e Reggio Emilia, via Campi 183, 41100 Modena, Italy.
出版信息
J Med Chem. 2005 Feb 24;48(4):913-6. doi: 10.1021/jm0491445.
PMID:15715461
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.
摘要
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