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J Med Chem. 2005 Feb 24;48(4):913-6.

Improving specificity vs bacterial thymidylate synthases through N-dansyl modulation of didansyltyrosine.

Author information

1
Dipartimento di Scienze Farmaceutiche, Università degli Studi di Modena e Reggio Emilia, via Campi 183, 41100 Modena, Italy. tondid@unimore.it

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.

PMID:
15715461
DOI:
10.1021/jm0491445
[Indexed for MEDLINE]

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