INVESTIGADORES
VILLANOVA Gabriela Vanina
congresos y reuniones científicas
Título:
3D Structure of T. cruzi bromodomain protein as potential drug design targets for Chagas.
Autor/es:
GOMEZ BARROSO JA; VILLANOVA GV; JEREZ B; STRADELLA F; SERRA E; AGUILAR CF
Lugar:
Mar del Plata, Buenos Aires, Argentina
Reunión:
Congreso; XLIII Reunión Anual SAIB; 2007
Institución organizadora:
Sociedad Argentina de Investigación Bioquímica y Biología Molecular
Resumen:
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Introduction: Trypanosoma cruzi is the etiologic agent of Chagas´disease. The proteins implicated in T. cruzi bromodomains are potential targets for drug design. The objective of our work is the resolution by X-ray crystallography of the three-dimensional structure of these proteins as a first step for rational drug design based on the structure. Materials and methods: The T. cruzi proteins under study are TcBDF2 (bromodomain factor 2) and TcBDF3 (bromodomain factor 3). They have been overexpressed in E. coli as an N-terminal fusion His-tag protein. The proteins have been obtained in native form and purified by Ni-sepharose affinity chromatography. The forlding status was evaluated by Native-PAGE and Urea-PAGE. Cristallyzation screenings of his-TcBDF3 have been carried out by microbatch under oil with and without N-acetyl Lysine. Results and discussion: His-TcBDF2 and TcBDF3 have been overexpressed and purified up to a concentration of > 20 mg/ ml. Electrophoretic assays have confirmed that the proteins are in native state. preliminary crystallization screenings are under way.
