ArticleCell stress & chaperones2026
The barcoded binding assay: Multiplexed profiling of chaperone binding selectivity for hydrophobic substrates.
Article in Cell stress & chaperones, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Membrane proteins contain hydrophobic sequences that must be chaperoned during protein folding and transport to the lipid bilayer. Failures in this essential process result in the formation of potentially toxic aggregates. Our mechanistic understanding of how chaperones interact with hydrophobic sequences is limited due to the technical challenges of measuring interactions between aggregation-prone proteins in a detergent-free environment. As hydrophobic substrates are prone to non-specific interactions, traditional binding assays that utilize one substrate and one chaperone per assay struggle to demonstrate that an interaction is specific and physiological. To address these technical challenges, we developed the barcoded binding assay, which allows for the measurement of chaperone binding selectivity to a complex pool of substrates in a detergent-free environment. In this assay, a pool of
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