Speaker Biography

Prof. Miroslav Pohanka

University of Defence, Czech Republic.

Title: Celecoxib inhibits acetylcholinesterase: an importance for neurological disorders

Prof. Miroslav Pohanka
Biography:

Prof. Dr. Miroslav Pohanka graduated from chemistry in Masaryk University Brno (Czech Republic) in 2003. In the Masaryk University, he achieved doctor of natural science (RNDr) from biochemistry in 2006 and PhD from biochemistry in 2008.  After that, he achieved associated professor (from toxicology at University of Defense, Czech Republic (2012) and doctor of sciences from analytical chemistry at Academy of Sciences, Czech Republic (2014) and professor from analytical chemistry at University of Pardubice (2016). He is an author of more than 200 papers in journals with IF and his works were more than 2000 times cited according web of science.

Abstract:

Celecoxib is a nonsteroidal anti-inflammatory drug which was introduced in the 1990s. It is known as an inhibitor of enzyme cyclooxygenase-2. The drug was introduced in 1990s. In the work presented here, affinity of celecoxib to enzyme acetylcholinesterase (AChE) is inferred because of structural motives in the celecoxib that make it resembling some inhibitors of AChE. Practical impact of properties coming from pertinent inhibition of AChE are proposed. .

Inhibition of human AChE by celecoxib was tested using standard spectrophotometric method and Dixon plot for inhibition constants calculation. Interaction between AChE and celecoxib was also predicted by molecular docking using Swiss dock software. 

A non-competitive mechanism of inhibition was revealed and equilibrium inhibitory constant equal to 313±40 µmol/l was determined. Comparing to AChE, inhibition of butyrylcholinesterase by celecoxib was not found. The lowest DG for complex celecoxib-AChE was equal to -7.78 kcal/mol. In this case, sulfonamide moiety of celecoxib was stacked between TYR 337 and TYR 341 of alfa anionic subsite of active site in the AChE. Cation-Π interactions appears to be responsible for the binding of celecoxib in the active site of AChE.

Though the here revealed and characterized inhibition has lower effect in real conditions than inhibition of cyclooxygenase. The finding is relevant for therapy of neurodegenerative disorders and some other specific pathologies. The inhibition of AChE by celecoxib can be utilized in the therapy of degenerative disorders like Alzheimer disease or it can be used as a prophylactic for poisoning by nerve agents.

This work was supported by a Ministry of Defence of the Czech Republic - long-term organization development plan Medical Aspects of Weapons of Mass Destruction of the Faculty of Military Health Sciences, University of Defence.