English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Background  Today, there is a growing recognition in the scientific community of the many roles of butyrylcholinesterase (BChE) in both physiological and pathological contexts.    Objective  Here, we aim at providing an accurate and comprehensive understanding of the mechanistic and structural aspects of mammalian BChE inhibition by the tricyclic antidepressant amitriptyline (AMI).    Materials and methods  The present work involves enzyme kinetic studies as well as protein–ligand docking and interaction profiling studies.    Results  We verify that AMI acts as an effective, mixed-type inhibitor of mammalian BChE, with an  IC  50  value of 10 μM and a  K  i  value of 2.25 μM. We also provide evidence showing that AMI penetrates deep into the active-site gorge of BChE where it interacts noncovalently with both the choline-binding and catalytic residues.    Conclusion  These findings could facilitate the prevention of the adverse metabolic sequelae of acquired BChE deficiency and also the design of new reversible anticholinesterase drugs.

New insights into the interaction between mammalian butyrylcholinesterase and amitriptyline: a combined experimental and computational approach