Quinoxaline as Dual Modulators of Apoptotic Regulators Bcl-2 and Bax: A Combined In Vitro and In Silico Anticancer...

This study aimed to evaluate the antioxidant potential of quinoxaline and investigate its molecular interactions with cancer-related proteins through computational docking.

Antioxidant activity of quinoxaline was assessed using DPPH, FRAP, ABTS, hydrogen peroxide, superoxide, and reducing power assays at varying concentrations, and IC₅₀ values were calculated. Molecular docking studies were performed to examine the interactions of quinoxaline with cancer-associated proteins, including epidermal growth factor receptor (EGFR), B-cell lymphoma 2 (Bcl-2), Bcl-2-associated X protein (Bax), and β-actin.

Antioxidant assays showed a concentration-dependent increase in inhibitory activity, with IC₅₀ values of 130.446 µM (DPPH), 151.343 µM (FRAP), 171.551 µM (ABTS), 108.194 µM (H₂O₂), 104.592 µM (superoxide), and 95.893 µM (reducing power assay). Molecular docking analysis revealed that quinoxaline exhibited strong binding affinity with the anti-apoptotic Bcl-2, suggesting potential inhibition of its function. Additionally, favorable interactions with the pro-apoptotic Bax were observed, indicating a possible dual mechanism of apoptosis induction.

Quinoxaline demonstrated significant antioxidant activity and potential pro-apoptotic effects by targeting key apoptotic regulators. The docking results suggest that quinoxaline could inhibit anti-apoptotic Bcl-2 while promoting the activity of the pro-apoptotic Bax, thereby inducing apoptosis and highlighting its potential as a promising anticancer agent.