ArticleChemical communications (Cambridge, England)2024
An organometallic swap strategy for bottlebrush polymer-protein conjugate synthesis.
Article in Chemical communications (Cambridge, England), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- Antibody-bottlebrush prodrug conjugates for targeted cancer therapy.Nature biotechnology · 2026Article
- Synergistic Effects of Polycationic and Polyfluorinated Functionalities for Efficient Intracellular Protein Delivery.Biomacromolecules · 2025Article
- Comparison of Cyclic and Linear PEG Conjugates.Bioconjugate chemistry · 2024Article
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Authors and funding
10 authors at 2 institutions in 1 country.
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Abstract
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.
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