Journal article
Thermodynamic and NMR analysis of inhibitor binding to dihydrofolate reductase
Abstract
Isothermal titration calorimetry (ITC) was used to determine the thermodynamic driving force for inhibitor binding to the enzyme dihydrofolate reductase (DHFR) from Escherichia coli. 1,4-Bis-{[N-(1-imino-1-guanidino-methyl)]sulfanylmethyl}-3,6-dimethyl-benzene (1) binds DHFR:NADPH with a K(d) of 13±5 nM while the related inhibitor 1-{[N-(1-imino-guanidino-methyl)]sulfanylmethyl}-3-trifluoromethyl-benzene (2) binds DHFR:NADPH with a K(d) of …
Authors
Batruch I; Javasky E; Brown ED; Organ MG; Johnson PE
Journal
Bioorganic & Medicinal Chemistry, Vol. 18, No. 24, pp. 8485–8492
Publisher
Elsevier
Publication Date
December 2010
DOI
10.1016/j.bmc.2010.10.048
ISSN
0968-0896