Artículos de revistas
Mapping molecular binding by means of conformational dynamics measurements
Fecha
2018-01-01Registro en:
RSC Advances, v. 8, n. 2, p. 867-876, 2018.
2046-2069
10.1039/c7ra10617c
2-s2.0-85040308023
2-s2.0-85040308023.pdf
Autor
Universitat Politècnica de València Camino de Vera
Universidade Estadual Paulista (Unesp)
Universitat de València
Institución
Resumen
Protein-protein interactions are key in virtually all biological processes. The study of these interactions and the interfaces that mediate them play a key role in the understanding of biological function. In particular, the observation of protein-protein interactions in their dynamic environment is technically difficult. Here two surface analysis techniques, dual polarization interferometry and quartz crystal microbalance with dissipation monitoring, were paired for real-time mapping of the conformational dynamics of protein-protein interactions. Our approach monitors this dynamics in real time and in situ, which is a great advancement within technological platforms for drug discovery. Results agree with the experimental observations of the interaction between the TRIM21α protein and circulating autoantibodies via a bridging bipolar mechanism. This work provides a new chip-based method to monitor conformational dynamics of protein-protein interactions, which is amenable to miniaturized high-throughput determination.