ArticleBioinformation2023
Insights from the molecular docking and simulation analysis of P38 MAPK phytochemical inhibitor complexes.
Article in Bioinformation, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Molecular dynamics and free energy analysis of curcumin binding near the DNA-recognition interface of NF-κB.Scientific reports · 2026Article
- In silico pharmacological analysis of Tinospora cordifolia compounds targeting African swine fever virus B175L.PloS one · 2026Article
- In Silico and In Vitro Evaluation of δ-cadinene fromCancers · 2025Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is of interest to develop p38α MAPK inhibitors. Docking, ADMET properties calculation, molecular dynamics, and MM-PBSA approaches were used to investigate the therapeutic potentials of p38α MAPK in complex with SB203580 (1A9U). The photo-molecules metergoline, withaphysacarpin, philadelphicalactone, canthin-6-one 9-glucoside, and SB-21600011 demonstrated high binding affinity compared to the reference drug. Furthermore, ADME profiles validated the drug-like properties of the prioritized phyto-compounds. Besides that, MD simulations were performed along with reference inhibitors for withaphysacarpin and metergoline to assess stability. Binding free energy calculations (MM-PBSA) revealed that metergoline and withaphysacarpin had estimated values (G) of 97.151 ± 21.023 kJ/mol and -82.084 ± 15.766 kJ/mol, respectively. In this study, metergoline and withaphysacarpin were found to have high affinity against p38α MAPK when compared to the reference compound SB 203580.
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