ArticleACS chemical biology2026
Development of m6A Readers for Enhanced Recognition In Vitro via Genetic Code Expansion.
Article in ACS chemical biology, 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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8 authors.
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Abstract
The YTH domain was recently demonstrated as a promising tool for recognizing and regulating m6A-modified RNAs. However, the deficiency in binding affinity (micromolar range) and selectivity (off-target binding) for m6A of the wild-type YTH domain limit its sensitivity and accuracy for m6A recognition. Engineering strategies for improving the affinity and selectivity of such epitranscriptomic readers remain lacking. Here, we demonstrate that site-specific introduction of noncanonical tryptophan derivatives within the aromatic m6A-binding pocket of the YTH domain modulates the binding affinity and selectivity. Specifically, we report two YTH variants, with 5-bromotryptophan and 5-hydroxytryptophan incorporated at the W465 of the YTH domain of YTHDF1, which show improved binding affinity and selectivity against m6A-modified RNAs. DFT-based energy decomposition analysis indicates that the binding affinity can be modulated through the substitution group's effect on the dispersion force in the van der Waals recognition complex, suggesting a critical role of the CH-π interaction in m6A-reader recognition. This work reports new reader domains with improved m6A recognition and demonstrates the potential of m6A reader engineering via genetic code expansion.
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