Receptor-based design of dihydrofolate reductase inhibitors: Comparison of crystallographically determined enzyme binding with enzyme affinity in a series of carboxy-substituted trimethoprim analogues

DOI: 10.1021/jm00381a008

Source and publish data:

Journal of Medicinal Chemistry p. 303 - 310 (1985)

Update date:2022-08-04

Topics:

Authors:

Kuyper Kuyper

Roth Roth

Baccanari

Ferone Ferone

Beddell Beddell

Champness

Stammers

Dann Dann

Norrington

Baker Baker

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Article abstract of DOI:10.1021/jm00381a008

By the use of molecular models of Escherichia coli dihydrofolate reductase (DHFR), analogues of trimethoprim (TMP) were designed which incorporated various 3'-carboxyalkoxy moieties in order to acquire ionic interactions with positively charged active-sit

Full text of DOI:10.1021/jm00381a008

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