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Influence of Enantiomeric Inhibitors on the Dynamics of Acetylcholinesterase Measured by Elastic Incoherent Neutron Scattering
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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2018 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 122, no 36, p. 8516-8525Article in journal (Refereed) Published
Abstract [en]

The enzyme acetylcholinesterase (AChE) is essential in humans and animals because it catalyzes the breakdown of the nerve-signaling substance acetylcholine. Small molecules that inhibit the function of AChE are important for their use as drugs in the, for example, symptomatic treatment of Alzheimer's disease. New and improved inhibitors are warranted, mainly because of severe side effects of current drugs. In the present study, we have investigated if and how two enantiomeric inhibitors of AChE influence the overall dynamics of noncovalent complexes, using elastic incoherent neutron scattering. A fruitful combination of univariate models, including a newly developed non-Gaussian model for atomic fluctuations, and multivariate methods (principal component analysis and discriminant analysis) was crucial to analyze the fine details of the data. The study revealed a small but clear increase in the dynamics of the inhibited enzyme compared to that of the noninhibited enzyme and contributed to the fundamental knowledge of the mechanisms of AChE-inhibitor binding valuable for the future development of inhibitors.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018. Vol. 122, no 36, p. 8516-8525
National Category
Pharmacology and Toxicology
Identifiers
URN: urn:nbn:se:umu:diva-152405DOI: 10.1021/acs.jpcb.8b05485ISI: 000444922800003PubMedID: 30110543OAI: oai:DiVA.org:umu-152405DiVA, id: diva2:1253635
Funder
Swedish Research Council, 2014-4675Available from: 2018-10-05 Created: 2018-10-05 Last updated: 2018-10-05Bibliographically approved

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Andersson, C. DavidLinusson, Anna

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