title: Analysis of Bacillus anthracis nucleoside hydrolase via in silico docking with inhibitors and molecular dynamics simulation.
abstract: As the enzyme nucleoside hydrolase (NH) is widely found in nature but has not yet been detected in mammals, it is considered an ideal target in the development of chemotherapy against parasitic diseases and bacterial infections like anthrax. Considering the risk that this biological warfare agent represents nowadays, the search for new drugs and new molecular targets in the development of chemotherapy against anthrax is imperative. On this basis, we performed docking studies of six known NH inhibitors at the active site of NH from Bacillus anthracis (BaNH). Subsequently, molecular dynamics (MD) simulations of these compounds inside BaNH were carried out in order to complement the docking studies and select the most promising compounds as leads for the design of potential BaNH inhibitors. Most of the docking and MD results obtained agreed well with each other and showed good correlation with experimental data.
authors.affiliation: Laboratory of Molecular Modeling Applied to Chemical and Biological Defense (LMCBD), Military Institute of Engineering, Rio de Janeiro, RJ, Brazil.
authors.forename: Ana P
authors.initials: AP
authors.lastname: Guimarães
authors.forename: Aline A
authors.initials: AA
authors.lastname: Oliveira
authors.forename: Elaine F F
authors.initials: EF
authors.lastname: da Cunha
authors.forename: Teodorico C
authors.initials: TC
authors.lastname: Ramalho
authors.forename: Tanos C C
authors.initials: TC
authors.lastname: França
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001408:Bacillus anthracis / Q000201:enzymology*; D020134:Catalytic Domain; D004791:Enzyme Inhibitors / Q000737:chemistry*; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
chemical_list: D004791:Enzyme Inhibitors; D009699:N-Glycosyl Hydrolases