Banca de QUALIFICAÇÃO: ANNA BEATRIZ SANTANA LUZ

Uma banca de QUALIFICAÇÃO de DOUTORADO foi cadastrada pelo programa.
STUDENT : ANNA BEATRIZ SANTANA LUZ
DATE: 05/01/2023
TIME: 09:00
LOCAL: Videoconferência - Link para acesso: https://meet.google.com/vgd-wqrn-hbe
TITLE:

Proteins: a systematic review of experimental models that mimic human digestion and in silico prospection of peptides with anti-SARS-CoV-2 potential

KEY WORDS:

Coronavirus; digestion; hydrolysis; protease inhibitors; pandemic; tamarind.

PAGES: 67
BIG AREA: Ciências Biológicas
AREA: Bioquímica
SUMMARY:

Proteins are important sources of essential amino acids. They can be hydrolyzed, generating peptides, which have various biological activities in the body. In this context, proteins have been used to generate products capable of treating numerous diseases, such as the coronavirus disease (COVID-19). To investigate experimental models that mimic human digestion and prospect peptides from trypsin inhibitor purified from tamarind (TTIp) seeds. The first two chapters of this study, referring to a systematic review (SR), are organized as follows: the first chapter presents the SR protocol registered in the International Prospective Register of Systematic Reviews (under number CRD42020198709); and the second chapter (still in progress) is the SR of in vitro studies that used methodological procedures to mimic the gastrointestinal digestion of proteins. Articles were selected according to the study population, interventions, control, results and type of study strategy and searches were carried out in Pubmed, Web of Science, Science direct, Embase, Virtual Health Library and Scopus databases. The methodological quality assessment was performed using the Office of Health Assessment and Translation tool. A total of 1.986 articles were selected, resulting in 20 eligible studies. In the results section, we describe the methodological procedures used in vitro to simulate the digestion of animal or vegetable proteins. The third chapter refers to an in silico prospecting study of native peptides and analogues with anti-SARS-Cov-2 potential, derived from TTIp. Native peptides were obtained from enzymatic cleavages of TTIp in silico and analogues were generated by replacing amino acids in the primary sequences of native peptides. The anti-SARS-CoV-2 potential was investigated by simulating molecular dynamics between the peptides and the binding sites of transmembrane serine protease 2 (TMPRSS2), responsible for the entry of SARS-CoV-2 into the host cell, and generated a patent application: BR 10 2022 020330 0. The best interaction potential energy occurred between TMPRSS2 and one of the native peptides obtained by cleavage with trypsin (-287.48 kJ.mol^-1) and its analogue peptide (-293.49 kJ.mol^-1). Thus, both peptides had many hydrophobic residues, a common physical-chemical property among peptides that inhibit the entry of enveloped viruses, such as SARS-Cov-2, present in specific drugs used to treat COVID-19. Therefore, this research presents an expressive scientific contribution, since the SR provided important data that will provide subsidies for development of studies related to the clinical application of bioactive peptides. In addition, the in silico study resulted, from the cleavage of TTIp 56/287, in potential candidates for agents that inhibit SARS-CoV-2 infection, encouraging future in vivo and in vitro investigations that aim to use the peptides prospected here as specific medicines for the treatment of COVID-19 and other diseases.

COMMITTEE MEMBERS:
Presidente - 1549705 - ADRIANA FERREIRA UCHOA
Externo à Instituição - NORBERTO DE KASSIO VIEIRA MONTEIRO - UFC