By Dr. Andrés Binolfi, IIDEFAR-CONICET
Next Wednesday 15 of June, to 11 hours, in the Auditorium of the Scientific Technological Center of Cordoba (CCT) then give the Lecture Series External Researchers "CIQUIBIC Open Doors".
In this opportunity, the lecture will be conducted by 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.
Design: Jeremías Di Pietro / Graphic design CCT CONICET CORDOBA
For the third “CIQUIBIC Open Doors” Lecture, CIQUIBIC is pleased to welcome Dr. Andres Binolfi, CONICET Associate Researcher at the Research Institute for Drug Discovery of Rosario (IIDEFAR), Argentina.
The conference will be held on Wednesday June 15, at 11 am in the Auditorium of the Scientific Technological Center CONICET (CCT-Córdoba).
Dr. Binolfi will lecture about
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.
Design: Jeremías Di Pietro / Graphical Design CCT CONICET CÓRDOBA