Anti-Aging Potential of Vitamin D: An Insilico Study
| dc.contributor.author | Tuntufye, Edna | |
| dc.date.accessioned | 2026-01-30T11:48:21Z | |
| dc.date.issued | 2025-02 | |
| dc.description | SDG: 3- Good Health and Well-Being SDG: 9- Industry, Innovation and Infrastructure | |
| dc.description.abstract | Despite extensive studies on the impact of vitamin D in aging retardation, the detailed atomic- level binding interactions between vitamin D (D2 and D3 forms) and associated anti-aging proteins have been largely unexplored. The study investigates these interactions by using molecular docking techniques to provide deeper insights into how vitamin D affects the structural dynamics and stability of the proteins associated with anti-aging process. The docking results reveal that vitamin D interacts most favorably with Sirt1 (PDB ID: 4zzi), a crucial anti-aging protein involved in DNA repair and metabolic regulation. Docking studies, including blind, grid, and hydrated docking approaches, show that vitamin D2 binds more strongly than vitamin D3 across all receptors evaluated. Specifically, in blind docking, vitamin D2 exhibited a binding affinity of −37.99 kJ/mol, while vitamin D3 showed a binding affinity of −34.85 kJ/mol. Grid docking revealed a similar trend, with vitamin D2 demonstrating a higher binding affinity of −41.38 kJ/mol compared to −40.08 kJ/mol for vitamin D3. These interactions are primarily hydrophobic, involving key residues such as Val445, Phe273, and Ala262 which form alkyl and pi-alkyl interactions with the ligands. The introduction of water molecules in hydrated docking further enhanced binding affinity, with vitamin D2 achieving an average binding free energy of −48.33 kJ/mol and vitamin D3 −45.94 kJ/mol highlighting the stabilizing effect of water in ligand-protein interactions. The Sirt1-vitamin D complexes maintained stable structural integrity with minimal RMSD and Rg fluctuations. The free energy surface revealed two preferred conformations for vitamin D2 and one for vitamin D3 indicating greater conformational flexibility for vitamin D2. The MM-PBSA results indicated that the vitamin D3-Sirt1 complex demonstrated superior stability, with a binding free energy of −167.12 ± 16.35 kJ/mol, compared to the vitamin D2-Sirt1 complex (−144.07±19.45). This suggests that vitamin D3 might have a more stable interaction with Sirt1, potentially offering enhanced therapeutic efficacy. The structural analysis revealed that both forms of vitamin D exhibited similar binding modes with vitamin D3 interacting at a lower energy than vitamin D2. These findings offer crucial insights into the molecular mechanisms underlying the role of vitamin D in aging, revealing key differences between vitamin D2 and D3 binding to Sirt1. | |
| dc.identifier.uri | https://dspace.nm-aist.ac.tz/handle/123456789/3656 | |
| dc.language.iso | en | |
| dc.publisher | NM-AIST | |
| dc.title | Anti-Aging Potential of Vitamin D: An Insilico Study | |
| dc.type | Thesis |