Targeting α7 nicotinic acetylcholine receptors and their protein interactions in Alzheimer's disease drug development
Open accessAbstract
The decades‐old cholinergic hypothesis of Alzheimer's disease (AD) led to clinical testing and FDA approval of acetylcholinesterase inhibitor drugs. Subsequently, the α7 nicotinic acetylcholine receptor (α7nAChR) was proposed as a new drug target for enhancing cholinergic neurotransmission. Nearly simultaneously, soluble amyloid β 1‐42 (Aβ 42) was shown to bind α7nAChR with picomolar affinity to activate kinases that hyperphosphorylate tau, the precursor to tau‐containing tangles. Multiple biopharmaceutical companies explored α7nAChR as a drug target for AD, mostly to enhance neurotransmission. Directly targeting α7nAChR proved to be a drug development challenge. The ultra‐high‐affinity interaction between Aβ 42 and α7nAChR posed a significant hurdle for direct competition in the AD brain. The receptor rapidly desensitizes, undermining efficacy of agonists. Drug discovery approaches therefore included partial agonists and allosteric modulators of α7nAChR. After substantial effort, numerous drug candidates were abandoned due to lack of efficacy or drug‐related toxicities. As alternatives, proteins interacting with α7nAChR were sought. In 2016, a novel nAChR regulator was identified, but no drug candidates have emerged from this effort. In 2012, the interaction of filamin A with α7nAChR was shown to be critical to Aβ 42's toxic signaling via α7nAChR, presenting a new drug target. The novel drug candidate simufilam disrupts the filamin A–α7nAChR interaction, reduces Aβ 42's high‐affinity binding to α7nAChR, and suppresses Aβ 42's toxic signaling. Early clinical trials of simufilam showed improvements in experimental CSF biomarkers and indications of cognitive improvement in mild AD patients at 1 year. Simufilam is currently in phase 3 clinical trials as a disease‐modifying treatment for AD.
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In AD brains, Simufilam binds with high-affinity FLNA stronger than native FLNA, reducing the affinity of Aβ42 with its receptor to the point where Aβ42 is displaced, preventing tau hyperphosphorylation and allowing microtubule stabilization.
“Indeed, in the AD brains, Simufilam binds with high-affinity FLNA stronger than native FLNA, reducing the affinity of Aβ42 with its receptor to the point where Aβ42 is displaced from its binding site. The tau hyperphosphorylation is prevented, allowing microtubule stabilization [162].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [162]
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- Authors
- Burns, L. H., Pei, Z., & Wang, H.
- Affiliations
- Cassava Sciences (United States) (US)
- City University of New York (US)
- Corresponding author
- Burns, Lindsay H.
- Venue
- Drug Development Research
- Publisher
- Wiley
- Published
- 2023-06-08
- Volume
- 84
- Issue
- 6
- Pages
- 1085-1095
- ISSN
- 0272-4391 (ISSN-L)
- 1098-2299
- OpenAlex
- W4379966714
- Cited by
- 35
- References
- 63
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 13 · 2023: 8
- FWCI
- 0.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Drug Development Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
- Keywords
- alpha7 nicotinic acetylcholine receptor, Alzheimer's disease, amyloid-beta 42, filamin A, receptor desensitization, partial agonists, allosteric modulators, tau hyperphosphorylation, cholinergic hypothesis, disease-modifying therapy, cerebrospinal fluid biomarkers
- MeSH terms
- Drug Development, Acetylcholinesterase, Alzheimer Disease, Cholinesterase Inhibitors, Humans, Spiro Compounds, Amyloid beta-Peptides, Filamins, alpha7 Nicotinic Acetylcholine Receptor
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