In the present work, we performed docking and molecular dynamics simulations studies on two groups of long-tailored oximes designed as peripheral site binders of acetylcholinesterase (AChE) and potential penetrators on the blood brain barrier. Our studies permitted to determine how the tails anchor in the peripheral site of sarin-inhibited human AChE, and which aminoacids are important to their stabilization. Also the energy values obtained in the docking studies corroborated quite well with the experimental results obtained before for these oximes.

b Faculty of Technology State University of Rio de Janeiro Rod Presidente Dutra Km 298 Pólo Industrial 27537 000 Resende RJ Brazil

c Chemistry Department Federal University of Viçosa Avenida Peter Henry Rolfs s n Campus Universitário Zip CPO Box Viçosa MG Brazil

Chemistry Department Federal University of Lavras PO Box 3037 37200 000 Lavras MG Brazil

e Federal Institute of Education Science and Technology Avenida Ministro Salgado Filho S Nº Bairro Soteco Zip Code 29106 010 Vila Velha Espírito Santo ES Brazil

f TNO Defense Security and Safety PO Box 45 2280 AA Rijswijk The Netherlands

g Faculty of Informatics and Management Center for Basic and Applied Research University of Hradec Kralove Hradec Kralove Czech Republic

h Department of Chemistry and Biochemistry Concordia University 7141 Sherbrooke W Montreal Canada

Laboratory of Molecular Modeling Applied to Chemical and Biological Defense Military Institute of Engineering Praça General Tibúrcio 80 22290 270 Rio de Janeiro Brazil

References provided by Crossref.org

Molecular Modeling Study of Uncharged Oximes Compared to HI-6 and 2-PAM Inside Human AChE Sarin and VX Conjugates

Design of inhibitors of thymidylate kinase from Variola virus as new selective drugs against smallpox: part II

Molecular Modeling and In Vitro Studies of a Neutral Oxime as a Potential Reactivator for Acetylcholinesterase Inhibited by Paraoxon

Molecular Modeling Studies on the Interactions of Aflatoxin B1 and Its Metabolites with Human Acetylcholinesterase. Part II: Interactions with the Catalytic Anionic Site (CAS)

Synthesis, Biological Evaluation, and Docking Studies of Novel Bisquaternary Aldoxime Reactivators on Acetylcholinesterase and Butyrylcholinesterase Inhibited by Paraoxon