μMap-uAA: Photocatalytic proximity labeling targeted with single-residue precision

Authors

Kang, M. S., Li, C., Buksh, B. F., Fernandez, D., MacMillan, D. W. C.

Abstract

Mapping protein microenvironments with residue-level precision in living cells remains challenging. We report Map-uAA, a genetically encoded proximity labeling platform that uses unnatural amino acid incorporation to install a tetrazine-quenched iridium photocatalyst at user-defined protein sites through click chemistry. Photocatalysis is activated by covalent attachment to the incorporated uAA, enabling localized catalytic labeling of proximal biomolecules. Applied to membrane receptors, Map-uAA captures domain- and time-dependent GPCR interaction networks with residue-level spatial precision.

Preprint server: bioRxiv
The authors list and abstract were imported from bioRxiv on 07 Aug 2026.

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