A comprehensive Conformational Análisis of Bullacin B, a Potent Inhibitor of Complex 1. Molecular Dynamics Simulations and Ab initio Calculations

J.A.BOMBASARO, M.F.MASMAN, L.N. SANTAGATA, M.L.FREILE, A.M.RODRIGUEZ, R.D.ENRIZ.

JOURNAL OF PHYSICAL CHEMISTRY A

Am. Chem Soc.

Lugar: Washington DC; Año: 2008 vol. 112 p. 7426 - 7428

1089-5639

Using a conformational systematic search combined with semiempirical and ab initio (RHF/3-21G and RHF/ 6-31G(d)) calculations, the conformational space of bullacin B was examined for the first time. In addition, molecular dynamics simulations were carried out to better evaluate the conformational behavior of this acetogenin. Our results indicate that bullacin B possesses a significant molecular flexibility. Although many different conformations were identified, at ab initio level, the L forms were energetically mostly preferred.  Our results support the use of molecular dynamics simulations for this compound suggesting that a combined decane/water system is a good solvent system to simulate the biological environment of this molecule acting as inhibitor of complex I.