Benzophenones and biflavonoids as inhibitors of pro-protein convertases

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

Abstract

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 an 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.(AU)