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Tercera conferencia del Ciclo “CIQUIBIC de puertas abiertas”

A cargo del Dr. Andrés Binolfi, IIDEFAR-CONICET

El próximo miércoles 15 de junio, a las 11 horas, en el Auditorio del Centro Científico Tecnológico de Córdoba (CCT) dará continuación el Ciclo de Conferencias de Investigadores Externos “CIQUIBIC de Puertas Abiertas”.
En esta oportunidad, la conferencia estará a cargo del Dr. Andrés Binolfi, Investigador Adjunto en el Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario, IIDEFAR-CONICET, Argentina.

Cellular structural biology of the protein alpha-synuclein

The structure and function of proteins depend on multiple cellular factors like localization, post-translational modifications, interactions with biological partners, etc. However, most protein structural studies are normally performed on isolated protein samples, under conditions that differ substantially from the crowded in vivo environments of intact cells. The question remains whether the features observed for proteins in vitro correlate with their cellular behavior. Until recently, there were no means of looking into live cells with high enough resolution to answer these questions. The development of in-cell nuclear magnetic resonance (NMR) techniques changed this notion. Here, I will show high-resolution in-cell NMR data on the structural and dynamic properties of the protein alpha-synuclein (AS), whose aggregation into amyloid fibrils is related to the onset of Parkinson´s disease (PD). By applying an electroporation approach to efficiently deliver isotopically enriched protein samples into the cytosol of cultured mammalian cells we delineated AS’s in vivo behaviors. In addition, by using oxidatively modified AS molecules, as observed in PD, we studied enzymatic redox repair pathways and identified permanently modified sites that might accumulate and exert neuronal toxicity under stress conditions. These results contribute to the understanding of the native conformations of AS and lays the ground for further in situ investigations of intracellular aggregation and PD related neurodegeneration.

Diseño: Jeremías Di Pietro / Diseño Gráfico CCT CONICET CÓRDOBA