Molecular Docking and Molecular Dynamics Simulation Studies of Triterpenes from Vernonia patula with the Cannabinoid Type 1 Receptor

A molecular docking approach was employed to evaluate the binding affinity of six triterpenes, namely epifriedelanol, friedelin, alpha-amyrin, alpha-amyrin acetate, beta-amyrin acetate, and bauerenyl acetate, towards the cannabinoid type 1 receptor (CB1). Molecular docking studies showed that friedelin, alpha-amyrin, and epifriedelanol had the strongest binding affinity towards CB1. Molecular dynamics simulation studies revealed that friedelin and alpha-amyrin engaged in stable non-bonding interactions by binding to a pocket close to the active site on the surface of the CB1 target protein. The studied triterpenes showed a good capacity to penetrate the blood-brain barrier. These results help to provide some evidence to justify, at least in part, the previously reported antinociceptive and sedative properties of Vernonia patula.

Automated summary

The molecular docking approach revealed that friedelin and alpha-amyrin had the strongest binding affinity towards CB1 and engaged in stable non-bonding interactions close to the active site. The triterpenes studied demonstrated good capacity to penetrate the blood-brain barrier, supporting the antinociceptive and sedative properties of Vernonia patula.