ArticleJACS Au2024
Highly Sensitive Labeling, Clickable Functionalization, and Glycoengineering of the MUC1 Neighboring System.
Article in JACS Au, 2024. 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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6 authors.
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Abstract
This study introduces a novel wash-type affinity-primed proximity labeling (WAPL) strategy for labeling and surface engineering of the MUC1 protein neighboring system. The strategy entails the utilization of peroxidase in conjunction with a MUC1-selective aptamer, facilitating targeted binding to MUC1 and inducing covalent labeling of the protein neighboring system. This study reveals a novel finding that the WAPL strategy demonstrates superior labeling efficiency in comparison to nonwash-type affinity-primed proximity labeling, marking the first instance of such observations. The WAPL strategy provides signal amplification by converting a single recognition event into multiple covalent labeling events, thereby improving the detection sensitivity for subtle changes in MUC1. The WAPL platform employs two levels of labeling upgrades, modifying the biotin handles of the conventional labeling substrate, biotin-phenol. The first level involves a range of clickable molecules, facilitating dibenzoazacyclooctynylation, alkynylation, and
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