Banca de QUALIFICAÇÃO: JOÃO PEDRO PORTILHO ENCIDE

Uma banca de QUALIFICAÇÃO de MESTRADO foi cadastrada pelo programa.
STUDENT : JOÃO PEDRO PORTILHO ENCIDE
DATE: 22/11/2023
TIME: 14:00
LOCAL: https://meet.google.com/dev-pewt-oiw
TITLE:

PROSPECTION OF PHYTOCHEMICALS IN MOLECULAR TARGETS VITAL TO THE LEISHMANIA INFANTUM CYCLE USING IN SILICO METHODS

PAGES: 30
BIG AREA: Ciências Exatas e da Terra
AREA: Química
SUBÁREA: Físico-Química
SPECIALTY: Química Teórica
SUMMARY:

Leishmaniasis is a group of diseases caused by protozoa of the genus Leishmania and can be fatal when left untreated. Leishmaniasis is considered by the World Health Organization to be a neglected disease, being endemic in Asia, Africa, the Americas and the Mediterranean region. Leishmania infantum is the etiological agent of visceral leishmaniasis (or kala-azar), affecting the internal organs of the infected person, with the female sandfly mosquito as its vector. Several pharmacological agents have been studied to treat this disease, with the investigation of phytochemicals and the area of drug design being extremely important for the development of leishmanicidal compounds. Molecular modeling methods are necessary to understand the behavior and function of proteins fundamental to the cycle of this protozoan and, using the molecular docking tool, estimate the possible modes of interaction between molecules with confirmed biological activity against L. infantum in the form amastigote (human infectious morphology) and possible related targets. Therefore, this project's main objective is to identify the biological targets available in the PDB repository and the possible mechanisms of inhibition of acetylated acetogenins with confirmed biological activity against this parasite. This data becomes useful for proposing structural modifications aimed at increasing the affinity of these ligands for their biological targets, as well as improving their physicochemical, toxicological and selectivity properties, making them more effective and reducing possible side effects. Possible metabolites were then estimated for each acetogenin and molecular docking calculations were carried out between the natural products and their predicted metabolites in the enzymes Trypanothione Reductase (TR) and Thiol-Dependent Reductase 1 (TDR1), hoping to find some pattern between them that explains their biological activities. Some metabolic products observed in the three acetogenins assumed similar conformations at the sites of these enzymes, suggesting a possible inhibition mechanism. 1 metabolite common to the three acetogenins was obtained for the FAD site in TR, 1 for the NADPH site also in TR and 2 for the TDR1 sites.

COMMITTEE MEMBERS:
Presidente - Interno ao Programa - 149.405.258-05 - KATHIA MARIA HONORIO - USP
Membro Titular - Examinador(a) Interno ao Programa - 1544394 - PAULA HOMEM DE MELLO
Membro Titular - Examinador(a) Externo à Instituição - VINICIUS GONCALVES MALTAROLLO - UFMG
Membro Suplente - Examinador(a) Interno ao Programa - 1544403 - MAURICIO DOMINGUES COUTINHO NETO