Banca de DEFESA: LUCAS MARQUES DE SOUZA

Uma banca de DEFESA de MESTRADO foi cadastrada pelo programa.
STUDENT : LUCAS MARQUES DE SOUZA
DATE: 30/10/2020
TIME: 09:00
LOCAL: Online
TITLE:

QUANTUM ANALYSIS OF THE INTERACTIONS BETWEEN THE AKR1D1 ENZYME AND THE STEROID HORMONES TESTOSTERONE AND PROGESTERONE

KEY WORDS:

AKR1D1; Steroid hormones; Testosterone; Progesterone; DFT; MFCC.

PAGES: 65
BIG AREA: Ciências Biológicas
AREA: Biofísica
SUBÁREA: Biofísica Molecular
SUMMARY:

The enzyme Δ4-3-cetosteroid 5β-Human Reductase (AKR1D1) is an essential regulator for bioavailability of steroids and metabolic phenotype. Its activity is directly related to diseases such as: obesity, type 2 diabetes mellitus, nonalcoholic fatty liver disease among others. Understanding how this enzyme works is of great importance to improve speed and efficiency in the development of disease treatments. Bearing this in mind, interactions between enzyme AKR1D1 with the two main masculine and feminine steroid hormones, testosterone and progesterone respectively, have been analyzed using quantum mechanics and computational simulation techniques the density functional theory (DFT) and the molecular fractionization with conjugate caps (MFCC) method. In the complex Testosterone AKR1D1 the amino acid residues that mostly contributed to attraction were: TRP230 > TYR26 > ASN227 > TYR132 > SER225; in complex Progesterone AKR1D1 they were: GLU120 > TRP230 > TYR58 > TYR132 > ILE57. The complex with Testosterone, located in the allosteric site of the protein, presented a higher energy of total interaction when compared to the location of progesterone in the active site. The residue TRP230 had a prominent role in both systems, reinforcing its important function of positioning the binder inside the enzyme. The GLU120, residue of the catalytic tetrad, showed the highest energy of interaction of AKR1D1 with progesterone.

BANKING MEMBERS:
Presidente - 1352009 - UMBERTO LAINO FULCO
Interno - 076.114.664-45 - JOSÉ XAVIER DE LIMA NETO
Externo à Instituição - PAULO HENRIQUE RIBEIRO BARBOSA - UFPI