Crystal structure, spectral investigations, DFT and antimicrobial activity of brucinium benzilate (BBA)

• Published in: Journal of molecular modeling Vol. 27; no. 8; p. 223
• Main Authors: Karnan, C., Nagaraja, K.S., Manivannan, S., Manikandan, A., Ragavendran, V.
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.08.2021; Springer Nature B.V
• Subjects: Antiinfectives and antibacterials; Characterization and Evaluation of Materials; Chemistry; Chemistry and Materials Science; Computer Appl. in Life Sciences; Computer Applications in Chemistry; Crystal structure; Energy gap; Hydrogen bonding; Molecular Medicine; Molecular orbitals; Nitrogen; Original Paper; Protonation; Salmonella; Surface analysis (chemical); Theoretical and Computational Chemistry; Brucinium benzilate; Spectroscopy; DFT; Antimicrobial properties; Crystal structure
• ISSN: 1610-2940; 0948-5023
• DOI: 10.1007/s00894-021-04842-w

The unreported brucinium benzilate (BBA) crystal and Hirshfeld surface analysis indicated the influence of intramolecular hydrogen bonding network on the crystal structure. Protonation occurs at the tertiary nitrogen as it is the most basic site. The protonated N-H + proton was observed at 7.08 ppm and the benzilate carbon COO - at 178.41 ppm. Molecular electrostatic potential (MEP) studies showed the electron-rich and electron-deficient sites in the molecule for understanding BBA interaction with an enzyme. Frontier molecular orbital (FMO) studies indicated that BBA molecule is thermodynamically stable and the HOMO-LUMO energy gap was found to be 4.454 eV. The highest interaction has the energy (322.86 kcal/mol) between tertiary ammonium N(LP) and H + . Inhibition tests showed that brucinium benzilate inhibits Bacillus cereus and Salmonella typhimurium bacteria. ADMET properties indicated that BBA has drug characteristics in binding plasma protein. Graphical abstract