Profiling the coulomb energy of chimanine D and desulphosinigrin as potential anti-diabetic drug against alpha-glucosidase

The structural aspect of target protein might become a new insight to evaluate the potencies of multiple compounds for drug discovery. The interaction and the composition of amino acids strongly influence many aspects, including the Coulomb energy of the ligand-protein complex system. Prediction of binding activity and molecular dynamics simulations of Averrhoa bilimbi's bioactive compounds for anti-diabetic agents were studied. The study demonstrated that chimanine D and desulphosinigrin have high potential drug-likeness properties to inhibit alpha-glucosidase activity. Further investigation through molecular dynamics simulation on both chimanine D and desulphosinigrin showed a stable pattern during simulation compared to the miglitol as control. These findings suggested that chimanine D or desulphosinigrin have one aspect as a possible anti-diabetic drug candidate. Future analysis, including the dynamic stability of the ligand-protein complex, protein stability during simulation, ligand movement, and ligand confirmation, need to be clarified.