Abstract

Acetylcholinesterase (AChE) is target enzyme of organophosphate (OP). Curent treatments for OP poisoning i.e. oximes, have limited success, especially without pre-treatment. This study uses molecular dynamic analysis to shine light on structure and dynamical fluctuations of free AChE and OP-inhibited AChE. Knowledge gained by the study of OP inhibition of acetylocholinesterase should guide future drug designs of more effective antitoxins.

Mentor

Brian Bennion

Lab site

Lawrence Livermore National Laboratory (LLNL)

Funding Acknowledgement

This material is based upon work supported by the S.D. Bechtel, Jr. Foundation and by the National Science Foundation under Grant No. 0952013. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the authors and do not necessarily reflect the views of the S.D. Bechtel, Jr. Foundation or the National Science Foundation. This project has also been made possible with support of the National Marine Sanctuary Foundation. The STAR program is administered by the Cal Poly Center for Excellence in Science and Mathematics Education (CESaME) on behalf of the California State University (CSU).

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URL: https://digitalcommons.calpoly.edu/star/210

 

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