Browsing by Author "Massanga, Caroline"

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    Exploring The Therapeutic Potential Of Urolithin A For Healthy Ageing: In Silico Study
    (NM-AIST, 2025-08) Massanga, Caroline
    Urolithin A, an active precursor derived from the metabolism of ellagitannins in rats and humans, is known for its potential health benefits, including stimulating mitophagy and promoting musculoskeletal function. While experimental studies have demonstrated Urolithin A’s potential to enhance cellular health, the detailed molecular interactions through which Urolithin A exerts its effects are not fully elucidated. Hence, this study investigated the anti inflammatory, anti-oxidation and neuro-protective abilities of Urolithin A in selected targets using molecular docking and molecular dynamics simulation methods. Molecular docking studies revealed the strong affinity for receptors involved in inflammation activities, including human p38 MAP kinase (4DLI) with ˉ10.1 kcal/mol interacting with SER252, LYS249 and ASP294 residues. The binding energy in the 5KIR target was ˉ8.6 kcal/mol, interacting with GLN203 through hydrogen bond, and lastly, 1A9U with an affinity of ˉ6.8 with no hydrogen bond formed with Urolithin A and interacts with van der Waals interactions. In oxidativetargets, the influence of Urolithin A was observed in 1OG5 with ˉ7.9 kcal/mol interacting with GLN185, PHE447. For the 1M17 target, the binding affinity was ˉ7.7 kcal/mol, interacting with THR95 residue and 1ZXM target at ˉ7.4 kcal/mol, interacting with TYR36, TYR216, and LEU234 residues. The neuro-protective ability of Urolithin A was observed in selected targets for acetyl cholinesterase; the binding energy was ˉ9.7 kcal/mol interacting with van der Waals and π der Waals and π interactions; for the 1GQR target, the binding energy was ˉ9.9 kcal/mol interacting with van interactions and for β-amylase (1iyt) the binding energy was ˉ5.5 forming hydrogen bond with SER8, GLN15 residues. Molecular Dynamics simulations at 100 ns of Urolithin A compared with reference 4DLI. The Urolithin A-4DLI complex exhibited greater stability than the reference receptor, as confirmed by RMSD, RMSF, Radius of Gyration, Hydrogen bond and SASA analyses.