| Grant number: | 24/00876-8 |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| Start date: | May 01, 2024 |
| End date: | April 30, 2026 |
| Field of knowledge: | Biological Sciences - Biophysics - Molecular Biophysics |
| Principal Investigator: | Paula Rahal |
| Grantee: | Carolina Gismene |
| Host Institution: | Instituto de Biociências, Letras e Ciências Exatas (IBILCE). Universidade Estadual Paulista (UNESP). Campus de São José do Rio Preto. São José do Rio Preto , SP, Brazil |
| Associated research grant: | 20/08615-8 - Protein exosites, cryptic sites and moonlighting: identification, functional mapping and effects of changes in structure, AP.TEM |
| Associated scholarship(s): | 25/02869-1 - Structural determination of the interaction between dengue virus NS1 and human prothrombin/thrombin: mapping critical exosites in the modulation of blood coagulation during infection, BE.EP.PD |
Abstract The interior of organisms constitutes a complex, crowded and dynamic environmentwith little semblance to the experiments conducted on isolated proteins. Data on the possibleinteractions that specific proteins can participate in within these crowded physiologicalenvironments is fundamental in understanding the multiple roles that are frequently played byproteins. High-resolution structural data have been instrumental in characterizing and definingthe stereochemical parameters that promote and define the binding of peptides, proteininhibitors and substrates at the active sites of enzymes to the point that we now have a verycomprehensive understanding of specific interactions and catalytic mechanisms whichfacilitate the design and development of highly selective synthetic inhibitors and drugs. On amore subtle level, protein surfaces often bristle with secondary binding sites (exosites), whichserve key roles in regulating and modulating diverse activities ranging from gene expression,conformational stabilization, transport, inhibition, and by extension, the modulation andexhibition of distinct functions or moonlighting by the same enzyme in response to changes inphysicochemical conditions are less well understood. This proposal combineshigh-throughput/high-resolution techniques such as phage display, metabolomics, structuralbiology, computational biology, along with fragment-based computational methods to map,select and evaluate protein surfaces and cryptic sites that specifically interact with peptidesand proteins and to identify the underlying dynamic protein-protein interactions that occurunder different physiological conditions. The core of this proposal is centered on proteins ofbiological relevance that are currently being studied in our research group to understand theirinteractions with peptides and with other proteins to discern their possible multiple roles. Thescientists participating in this research proposal have maintained an intensive exchangeprogram and have been successfully collaborating over a long period as evidenced by the jointpublications and patent applications. | |
| News published in Agência FAPESP Newsletter about the scholarship: | |
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