Description:
Superoxide dismutases (SODs) are metalloenzymes that defend the body against reactive oxygen species. Human cells have three distinct SODs, i.e., MnSOD, ECSOD, and Cu-ZnSOD (SOD1). Camellia sinensis L. leaves contain polyhydroxylated polyphenols in the form of catechins. This work aims to study the binding mode and molecular dynamics (MD) of epigallocatechin (EGC) and epigallocatechin gallate (EGCG) compared to ascorbic acid and SBL1 (native ligand) with SOD1. Molecular docking was performed using AutoDock 4.2. The complex stability and MM-GBSA were analyzed by trajectory analysis using Amber22. Both catechins demonstrated a binding mode with the enzyme, in terms of hydrogen bonds and hydrophobic interaction, similar to the SBL1. Meanwhile, ascorbic acid is only similar in hydrogen bonds. EGC and ascorbic acid possess a better binding affinity (-4.15 kcal/mol) compared to EGCG (-4.02 kcal/mol), thus the EGC/SOD1 complex was continued in 100 ns MD simulation. The MD simulation confirmed that EGC is more stable than the SBL1 with the RMSD average value of SBL1 and EGC being 1.1669 Å and 0.5607 Å, respectively. Taken together, this study confirms the antioxidant activity of catechins

URL:
http://103.158.96.210:88/web_repository/uploads/51034-203928-3-PB.pdf

Type:
Journal

Document:
Diploma III Farmasi

Date:
23-06-2024

Author:
LIDYA C BAWONO