INSTITUTO DE FISICA DE LIQUIDOS Y SISTEMAS BIOLOGICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Study of the molecular mechanisms associated to the dynamic and structural properties in the protein aggregation of TRP-cage
YANIS RICARDO ESPINOSA SILVA; C. GASTÓN FERRARA; FAUNDEZ CRISTIAN
Congreso; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; 2018
The study of the protein aggregation process is of vital importance to understand many of the biological events that occur in the cell. There are a series of conformational disorders in the folded protein that responsible for the appearance of pathologies such as type 2 diabetes or neurodegenerative-type disorders such as Alzheimer´s, Parkinson´s or Huntington´s disease, even being fatal as is the case of spongiform encephalopathies transmissible, for example, Creutzfeldt-Jakob disease.The molecular mechanisms that trigger these diseases are the result of the protein conformational disorders (DCP), a disorder that has received great attention in recent years. If we only take Parkinson´s disease as a reference, we would see that its prevalence is close to 2% in populations older than 65 years, which transforms this disease and the rest of the PCDs into a cause of growing concern for the general population.In the present work, we show the first results obtained from a dynamic and structural analyzes of the protein aggregation process of TRP-cage, where the all analyzes were performed using Molecular Dynamics simulations (DM). The systems studied formed aggregates composed of 2 to 4 proteins, under physiological conditions (saline concentration) and thermodynamic (temperature and pressure) stable, attempting to adequately represent the biological conditions of the process and how thermodynamic variations modify the kinetics of aggregation and the structure of the aggregate. The results show the analysis of the solvent exposed surfaces (SASA) of the proteins, of the proteins in the state of aggregation, of hydrophobic and hydrophilic groups, different amino acids, interdistance between the hydrophobic cores of the proteins, energies of interaction between groups, radial distribution functions and other parameters that characterize the dynamics and structure ofprotein aggregation.