Identificação e caracterização de novos criptídeos obtidos pela hidrólise da hemoglobina e suas atividades sobre a enzima conversora de angiotensina (EC 3.4.15.1) e a renina (EC 3.4.23.15)

Abstract

Cryptids are peptides with bioactive function that are hidden in other proteins, having similar or even different function from these mother proteins. The objective of this work is to analyze the generation of these cryptides from the hydrolysis of hemoglobin, which already has active peptides described as hemocidin, hemorphine and hemopressin, and to analyze their interaction with the enzymes ACE (Angiotensin Converting Enzyme) and Renin that are part of the system Renin- Angiotensin which is fundamental for cardio circulatory regulation. Hydrolysis of the hemoglobin was performed by trypsin, and the material was analyzed in SDS-Page and fractionated in High Pressure Liquid Chromatography. The mass of the peptides generated in LC-MS and in silico was determined. Preliminary tests were performed with ACE and the fractions, with results above 60% inhibition. The tests were redone in a fluorimetric assay again showing results above 60% inhibition in 4 fractions. The fluorimetric test was also used with the enzyme renin, with results around 20% inhibition. These same fractions were tested for MTT in fibroblast cell culture and no toxicity or proliferation was observed.