ArticleAnalytical chemistry2025
Fab-Induced Stabilization of an Ion Channel Receptor Enables Mechanistic Characterization of Small-Molecule Therapeutics.
Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- A Machine Learning-Enabled Venom Peptide Platform for Rapid Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2026Article
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Authors and funding
11 authors.
Funding
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Abstract
Developing small-molecule (SM) therapeutics that target membrane proteins (MPs) is often challenging, because few biophysical methods can handle the detergents required to maintain target stability. Here, we report a surface plasmon resonance (SPR)-based methodology that enables the characterization of interactions between SMs and an ion channel receptor (MP1) in complex with a stabilizing antibody fragment (Fab) and surfactant. Briefly, a stable MP1-Fab complex was formed by coimmobilizing MP1 with an anti-MP1-Fab within the hydrogel film to study the interactions of MP1 with SMs. The critical micelle concentration (CMC) is the concentration at which 50% of the surfactant monomers are assembled into micelles. Micelles readily absorb compounds resulting in compound-loaded micelles that generate high nonspecific binding and hinder resolution of SM binding responses. This micelle-induced interference was avoided by utilizing a weak detergent at a concentration below its CMC, allowing for the resolution of compound binding to a solvent-exposed pocket. Additional Fab stabilization was required to rescue binding at a second pocket buried within the transmembrane region of MP1. The resulting SPR-based assay proved invaluable during hit-to-lead optimization by progressing structure-activity relationship (SAR) studies and resolving the mechanism of action (MoA).
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