Autor: Krajcovicova, S.; Wharton, T.; Driscoll, C. L.; King, T. A.; Howarth, M. R.; Spring, D. R.
Název práce v češtině: A Platform for SpyCatcher Conjugation to Native Antibodies
Název práce v angličtině: A Platform for SpyCatcher Conjugation to Native Antibodies
Studentská publikace: ne
Klíčová slova v češtině: …
Klíčová slova v angličtině: …
Abstrakt česky: …
Abstrakt anglicky: Protein–antibody conjugates represent major advancements in targeted therapeutics. However, platforms enabling ‘off-the-shelf’ antibody conjugation are seldom reported. The SpyTag/SpyCatcher system, known for its stable isopeptide bond formation, is widely used to engineer protein architectures and study protein folding. This work introduces the fusion of SpyCatcher with native antibodies using cysteine-reactive tetra-divinylpyrimidine (TetraDVP)-SpyTag linkers. This platform allows for the rapid and stable conjugation of a native antibody with SpyCatcher proteins. As a proof of concept, the HER2-targeting antibody trastuzumab was conjugated to different SpyCatcher proteins using a TetraDVP-SpyTag linker, producing robust conjugates that retained specific binding to HER2-positive cells with excellent conversion rates. To demonstrate the platform’s broader applicability, the TetraDVP-SpyTag linker was successfully conjugated to additional native IgG1 and IgG4 antibodies (durvalumab, brentuximab, cetuximab, and gemtuzumab) with similarly high efficiency as trastuzumab. Moreover, a scalable solid-phase synthesis of TetraDVP linkers has been developed, achieving high yields and purity. This innovative platform enables precise, single-step antibody bioconjugation, offering strong potential for protein–antibody conjugate synthesis. With applications across therapeutics and diagnostics, this method advances antibody-based drug development.
Jazyk v originále: angličtina
Název časopisu: Chemical Science
Rok: 2025
Svazek (ročník): 2025
Číslo časopisu v rámci uvedeného svazku: accepted article
Strana od-do: ,
Impact factor: 8
Q1: ano

ISSN časopisu: ,
Vydavatel: The Royal Society of Chemistry
Způsob financování: 22-07138O
DOI: https://pubs.rsc.org/en/content/articlelanding/2025/sc/d5sc02286j