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The Selectivity of Butyrylcholinesterase Inhibitors Revisited.

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Title: The Selectivity of Butyrylcholinesterase Inhibitors Revisited.
Authors: Gambardella, Michael D., Wang, Yigui, Pang, Jiongdong
Source: Molecules; Nov2025, Vol. 30 Issue 21, p4201, 35p
Subject Terms: BUTYRYLCHOLINESTERASE, ALZHEIMER'S disease, DRUG approval, THERAPEUTICS, CHOLINERGIC mechanisms, CHOLINESTERASE inhibitors, AMYLOID beta-protein
Abstract: Acetylcholinesterase (AChE) inhibitors are the primary target for single-molecule anti-Alzheimer's disease (AD) therapeutics. Though AChE has historically been the focus of investigation for small-molecule inhibitors, interest in another cholinergic enzyme, butyrylcholinesterase (BChE), has grown in recent years. Attention stems from BChE's role in β-amyloid (Aβ) protein aggregation and an increase in BChE concentration during the late stages of AD, where a decrease in AChE concentration is also observed. Currently, five FDA-approved drugs are on the market for inhibiting AChE, though no BChE-selective drugs have been approved so far. In this review, we focus on newly identified BChE selective inhibitors and present the ideas behind these discoveries. [ABSTRACT FROM AUTHOR]
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Database: Complementary Index
Description
Abstract:Acetylcholinesterase (AChE) inhibitors are the primary target for single-molecule anti-Alzheimer's disease (AD) therapeutics. Though AChE has historically been the focus of investigation for small-molecule inhibitors, interest in another cholinergic enzyme, butyrylcholinesterase (BChE), has grown in recent years. Attention stems from BChE's role in β-amyloid (Aβ) protein aggregation and an increase in BChE concentration during the late stages of AD, where a decrease in AChE concentration is also observed. Currently, five FDA-approved drugs are on the market for inhibiting AChE, though no BChE-selective drugs have been approved so far. In this review, we focus on newly identified BChE selective inhibitors and present the ideas behind these discoveries. [ABSTRACT FROM AUTHOR]
ISSN:14203049
DOI:10.3390/molecules30214201