YopH tyrosine phosphatase, a virulence factor produced by pathogenic species of Yersinia, is an attractive drug target. In this work, three oxidovanadium(IV) complexes were assayed against recombinant YopH and showed strong inhibition of the enzyme in the nanomolar range. Molecular modeling indicated that their binding is reinforced by H-bond, cation−π, and π–π interactions conferring specificity toward YopH. These complexes are thus interesting lead molecules for phosphatase inhibitor drug discovery.
Martins, P.G.A., Mori, M., Chiaradia Delatorre, L.D., Menegatti, A.C.O., Mascarello, A., Botta, B., et al. (2015). Exploring oxidovanadium(IV) complexes as YopH inhibitors: mechanism of action and modeling studies. ACS MEDICINAL CHEMISTRY LETTERS, 6(10), 1035-1040 [10.1021/acsmedchemlett.5b00267].
Exploring oxidovanadium(IV) complexes as YopH inhibitors: mechanism of action and modeling studies
MORI, MATTIA;
2015-01-01
Abstract
YopH tyrosine phosphatase, a virulence factor produced by pathogenic species of Yersinia, is an attractive drug target. In this work, three oxidovanadium(IV) complexes were assayed against recombinant YopH and showed strong inhibition of the enzyme in the nanomolar range. Molecular modeling indicated that their binding is reinforced by H-bond, cation−π, and π–π interactions conferring specificity toward YopH. These complexes are thus interesting lead molecules for phosphatase inhibitor drug discovery.
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https://hdl.handle.net/11365/1120426
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