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Master's Dissertation
DOI
10.11606/D.87.2017.tde-23052017-133753
Document
Author
Full name
Cristiane Castilho Fernandes da Silva
Institute/School/College
Knowledge Area
Date of Defense
Published
São Paulo, 2017
Supervisor
Committee
Portaro, Fernanda Calheta Vieira (President)
Casa, Maisa Splendore Della
Magalhães, Geraldo Santana
Title in Portuguese
Busca por polipeptídeos bioativos derivados da degradação do cininogênio, fibrinogênio e fibronectina pela bothropasina e Bothrops protease A.
Keywords in Portuguese
Cininogênio
Fibrinogênio
Fibronectina
Peptídeos bioativos
Protease do veneno
Abstract in Portuguese
Estudamos a ação das proteases bothropasina e Bothrops protease A, do veneno da serpente Bothrops jararaca, sobre o fibrinogênio (FBG), fibronectina (FN) e cininogênio (HK), como ferramenta para geração de peptídeos bioativos. As sequências primárias dos produtos de digestão foram identificadas por espectrometria de massas, com as buscas direcionadas por peptídeos em comum gerados pelas duas proteases. Foram encontradas oito sequências em comum provenientes do FBG e onze, da FN. Apenas a bothropasina clivou o HK, liberando desArg9BK. Foram sintetizados peptídeos derivados do FBG (FBG1-6) e da FN (FN1-4), além de des-Arg9-BK. Oito peptídeos apresentam potencial atividade antiangiogênica predita in silico. Observamos a inibição da elastase (28-20%) causada por FBG1-2-5-6. A melhor inibição da trombina foi de 17%, por FBG1. Contudo, a maioria dos peptídeos intensificou sua atividade. Por fim, este trabalho sugere que as proteases de veneno de serpentes podem ser usadas como ferramentas para processar componentes do plasma, visando à busca por peptídeos bioativos.
Title in English
Search for bioactive derived degradation polypeptides of kininogen, fibrinogen and fibronectin by bothropasin and Bothrops protease A.
Keywords in English
Fibrinogen
Fibronectin
Kininogen
Peptides bioactive
Venom protease
Abstract in English
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.
 
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Publishing Date
2017-05-23
 
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