Advanced search
Start date
Betweenand


Search for bioactive derived degradation polypeptides of kininogen, fibrinogen and fibronectin by bothropasin and Bothrops protease A.

Full text
Author(s):
Cristiane Castilho Fernandes da Silva
Total Authors: 1
Document type: Master's Dissertation
Press: São Paulo.
Institution: Universidade de São Paulo (USP). Instituto de Ciências Biomédicas (ICB/SDI)
Defense date:
Examining board members:
Fernanda Calheta Vieira Portaro; Maisa Splendore Della Casa; Geraldo Santana Magalhães
Advisor: Fernanda Calheta Vieira Portaro
Abstract

We studied the action of the proteases bothropasin and Bothrops protease A purified from the venom of snake Bothrops jararaca upon fibrinogen (FBG), fibronectin (FN) and kininogen (HK), as a tool to generate bioactive peptides. The primary sequences of the digestion products were identified by mass spectrometry and we focused the search for common peptides released by both proteases simultaneously. Sequences in common released by both proteases were found, being eight peptides from FBG, and 11 from FN. Only bothropasin was able to cleave HK releasing des-Arg9-BK. Peptides from fibrinogen (FBG1-6) and from fibronectin (FN1-4), as well as the des-Arg9-BK were synthetized. Eight peptides have potential antiangiogenic predicted in silico. We observed the inhibition of elastase (28-20%) caused by FBG1-2-5-6. The best inhibition of thrombin was 17% by FBG1. However, most of the peptides intensified its activity. Finally, this work suggests that the snake venom protease can be used as tools to process plasma components in order to search for bioactive peptides. (AU)

FAPESP's process: 14/02788-7 - Characterization of polypeptide modulators of angiogenesis derived from the degradation of kininogen and fibrinogen by Bothropasin
Grantee:Cristiane Castilho Fernandes da Silva
Support Opportunities: Scholarships in Brazil - Master