Mapping molecular binding by means of conformational dynamics measurements

• Autor(a) principal: Do Nascimento, Noelle M.
• Data de Publicação: 2018
• Outros Autores: Juste-Dolz, Augusto, Bueno, Paulo R. [UNESP], Monzó, Isidro, Tejero, Roberto, Lopez-Paz, José L., Maquieira, Angel, Morais, Sergi, Gimenez-Romero, David
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNESP
• Texto Completo: http://dx.doi.org/10.1039/c7ra10617c; http://hdl.handle.net/11449/175732

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.