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Chiaradia-Delatorre L.D.,Laboratorio Estrutura e Atividade LEAT | De Oliveira K.N.,Laboratorio Estrutura e Atividade LEAT | Guido R.V.C.,University of Sao Paulo | Andricopulo A.D.,University of Sao Paulo | And 2 more authors.
European Journal of Medicinal Chemistry | Year: 2013

YopH plays a relevant role in three pathogenic species of Yersinia. Due to its importance in the prevention of the inflammatory response of the host, this enzyme has become a valid target for the identification and development of new inhibitors. In this work, an in-house library of 283 synthetic compounds was assayed against recombinant YopH from Yersinia enterocolitica. From these, four chalcone derivatives and one sulfonamide were identified for the first time as competitive inhibitors of YopH with binding affinity in the low micromolar range. Molecular modeling investigations indicated that the new inhibitors showed similar binding modes, establishing polar and hydrophobic contacts with key residues of the YopH binding site. © 2013 Elsevier Inc. All rights reserved.

Masteloto H.G.,Campus Universitario | Drawanz B.B.,Campus Universitario | Berwaldt G.A.,Campus Universitario | Neuenfeldt P.D.,Laboratorio Estrutura e Atividade LEAT | And 2 more authors.
Monatshefte fur Chemie | Year: 2015

New 2-aryl-3-(benzo[d][1,3]dioxol-5-yl)thiazolidin-4-ones were easily synthesized by one-pot reaction of (3,4-methylenedioxy)aniline, arenaldehydes (or cyclohexanone), and mercaptoacetic acid which results in good yields. The thiazolidinones were fully identified and characterized by spectroscopic techniques as 1H and 13C NMR, mass and high resolution mass. These novel heterocycles are potential biological compounds due the presence of both important moieties: thiazolidinone and 1,3-benzodioxole. © 2014 Springer-Verlag Wien.

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