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Benzophenones and Biflavonoids as Inhibitors of Pro-protein Convertases

Grant number: 11/20291-4
Support type:Scholarships in Brazil - Scientific Initiation
Effective date (Start): December 01, 2011
Effective date (End): November 30, 2013
Field of knowledge:Biological Sciences - Biochemistry - Enzymology
Principal Investigator:Wagner Alves de Souza Júdice
Grantee:Gerson Profeta de Souza
Home Institution: Pró-Reitoria de Pesquisa, Pós-Graduação e Extensão. Universidade de Mogi das Cruzes (UMC). Mogi das Cruzes , SP, Brazil


The catalytic mechanism of serine proteases is based on the catalytic triad of the active site, consisting of three invariable amino acids: serine, which acts as a nucleophilic group, aspartate, and histidine as electrophilic group acting as a base. In eukaryotes, several proteins that pass through the secretory pathway are synthesized as pro-proteins undergo endo- or exo-proteolysis. Are classic examples of secreted factors, such as insulin, membrane proteins can undergo this type of processing, such as the insulin receptor or gp 160 protein of HIV. This undergraduate research project aims to study the pro-protein convertases (Kex2, furin and PC1) against possible inhibitory molecules derived from benzophenones and biflavonoids groups which are natural molecules that have been chemically modified.