Anti-Parkinson Drug Biperiden Inhibits Enzyme Acetylcholinesterase.

Biperiden is a drug used in Parkinson disease treatment and it serves also as an antiseizures compound in organophosphates poisoning. It acts as antagonist of muscarinic receptor activated by acetylcholine while the enzyme acetylcholinesterase (AChE) cleaves acetylcholine in synaptic junction into c...

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Publicado en:BioMed Research International Vol. 2017; pp. 1 - 6
Autores principales: Kostelnik, Adam, Cegan, Alexander, Pohanka, Miroslav
Formato: equations & formulas research tables/charts Journal Article
Publicado: Wiley-Blackwell 7/13/2017
Acceso en línea:Ver este registro en EBSCOhost
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      dt: 7/13/2017
      vid: 2017
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      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        124092487
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        10.1155/2017/2532764
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        atl: Anti-Parkinson Drug Biperiden Inhibits Enzyme Acetylcholinesterase.
      aug:
        au:
          Kostelnik, Adam
          Cegan, Alexander
          Pohanka, Miroslav
        affil: Faculty of Chemical Technology, University of Pardubice, Studentska 95, 53210 Pardubice, Czech Republic
      sug:
        subj:
          Antiparkinson Agents Therapeutic Use
          Acetylcholinesterase Physiology
          Human
          Seizures Prevention and Control
          Enzymes
          Drug Interactions
          Computer Systems
          Cholinergic Antagonists Administration and Dosage
          Data Analysis Software
          Funding Source
      ab: Biperiden is a drug used in Parkinson disease treatment and it serves also as an antiseizures compound in organophosphates poisoning. It acts as antagonist of muscarinic receptor activated by acetylcholine while the enzyme acetylcholinesterase (AChE) cleaves acetylcholine in synaptic junction into choline and acetic acid. This enzyme is inhibited by various compounds; however there has not been proposed evidence about interaction with biperiden molecule. We investigated this interaction using standard Ellman’s assay and experimental findings were critically completed with an in silico prediction by SwissDock docking software. Uncompetitive mechanism of action was revealed from Dixon plot and inhibition constant (Ki) was calculated to be 1.11 mmol/l. The lowest predicted binding energy was −7.84 kcal/mol corresponding to H-bond between biperiden molecule and Tyr 341 residuum in protein structure of AChE. This interaction seems to be further stabilized by π-π interaction with Tyr 72, Trp 286, and Tyr 341. In conclusion, biperiden appears as a very weak inhibitor but it can serve as a lead structure in a pharmacological research.
      pubtype: Academic Journal
      doctype:
        equations & formulas
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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