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Polymer–protein bioconjugation offers a powerful strategy to alter the physical properties of proteins, and various synthetic polymer compositions and architectures have been investigated for this purpose. Nevertheless, conjugation of molecular bottlebrush polymers (BPs) to proteins remains an unsolved challenge due to the large size of BPs and a general lack of methods to transform the chain ends of BPs into functional groups suitable for bioconjugation. Here, we present a strategy to address this challenge in the context of BPs prepared by "graft-through" ring-opening metathesis polymerization (ROMP), one of the most powerful methods for BP synthesis. Quenching ROMP of PEGylated norbornene macromonomers with an activated enyne terminator facilitates the transformation of the BP Ru alkylidene chain ends into Pd oxidative addition complexes (OACs) for facile bioconjugation. This strategy is shown to be effective for the synthesis of two BP–protein conjugates (albumin and ERG), setting the stage for a new class of BP–protein conjugates for future therapeutic and imaging applications. [ABSTRACT FROM AUTHOR]

A commercially available naphthalene fluorophore serves as a ratiometric indicator for albumin, showcasing its applications in albumin-based supramolecular recognition. [ABSTRACT FROM AUTHOR]

A commercial anti-cancer drug, axitinib, exhibits very stable dual emissions for discrimination of human serum albumin. [ABSTRACT FROM AUTHOR]

The design of stable and variable aryl linkers for conjugating drug moieties to the metabolism-related thiols is of importance in drug discovery. We disclosed that thioimidazolium groups are unique scaffolds for the thiol–(hetero)arene conjugation under mild conditions. The drug bound thioimidazolium salts, which are easily accessible via a copper-mediated Chan–Lam process in gram-scale, could be successfully applied to the late-stage coupling of bioactive thiols to construct a broad array of drug-like molecules. [ABSTRACT FROM AUTHOR]

The first fluorescent sensor based on the indicator displacement assay (IDA) for on-site determination of etomidate. [ABSTRACT FROM AUTHOR]