Resveratrol inhibits Trypanosoma cruzi arginine kinase and exerts a trypanocidal activity

EDWARD A. VALERA VERA; FLAVIA S. DAMASCENO; CLAUDIO A. PEREIRA; CHANTAL REIGADA; MARIANA R. MIRANDA; MELISA MARTINEZ SAYÉ; ARIEL M. SILBER

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2016 vol. 87 p. 498 - 503

0141-8130

Arginine kinase catalyzes the reversible transphosphorylation between ADP and phosphoarginine which plays a critical role in the maintenance of cellular energy homeostasis. Arginine kinase from the protozoan parasite Trypanosoma cruzi, the etiologic agent of Chagas disease, meets the requirements to be considered as a potential therapeutic target for rational drug design including being absent in its mammalian hosts. In this study a group of polyphenolic compounds was evaluated as potential inhibitors of arginine kinase using molecular docking techniques. Among the analyzed compounds with the lowest free binding energy to the arginine kinase active site (