A Platform for SpyCatcher Conjugation to Native Antibodies
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F25%3A73632438" target="_blank" >RIV/61989592:15310/25:73632438 - isvavai.cz</a>
Result on the web
<a href="https://pubs.rsc.org/en/content/articlepdf/2025/sc/d5sc02286j" target="_blank" >https://pubs.rsc.org/en/content/articlepdf/2025/sc/d5sc02286j</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/D5SC02286J" target="_blank" >10.1039/D5SC02286J</a>
Alternative languages
Result language
angličtina
Original language name
A Platform for SpyCatcher Conjugation to Native Antibodies
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10401 - Organic chemistry
Result continuities
Project
<a href="/en/project/GN22-07138O" target="_blank" >GN22-07138O: Conformationally-constrained peptide-drug conjugates as a platform for targeted therapeutics</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Chemical Science
ISSN
2041-6520
e-ISSN
2041-6539
Volume of the periodical
16
Issue of the periodical within the volume
23
Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
10602-10609
UT code for WoS article
001488356500001
EID of the result in the Scopus database
2-s2.0-105005433532