ArticleBioconjugate chemistry2025
Genetic Engineering of VHH Antibody Fragments for Efficient Site-Specific Conjugation to Polysaccharides.
Article in Bioconjugate chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Development and Preliminary Evaluation of an OMP16-Targeting Trivalent Nanobody-HRP-Based cELISA for Serological Detection of Bovine Brucellosis.Animals : an open access journal from MDPI · 2026Article
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9 authors.
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Abstract
Site-selective modifications of proteins, without compromising their biological activity, are highly sought after due to their critical role in many biomedical applications. Here, we established a universal and efficient approach for site-selective conjugation of a variable domain of single-chain heavy-chain only antibody fragments (VHH) to polysaccharides using thiol-maleimide chemistry, known for its specificity and efficiency. This is achieved by genetically engineering an unpaired cysteine (Cys) residue in a C-terminal extension of VHHs. In this study, we synthesized two maleimide-functionalized polysaccharides, i.e., dextran-maleimide (Dex-Mal) and hyaluronic acid-maleimide (HA-Mal), for protein conjugation. Six distinct VHHs were selected and engineered with C-terminal extensions containing Cys residues for conjugation with Dex-Mal and HA-Mal. Conjugation efficiency varied among VHHs due to structural heterogeneity, which influenced the reactivity of the engineered Cys residues. One VHH, specific to TNFα (anti-TNFα-VHH), exhibited low conjugation efficiency (<20%); however, efficiency was fully restored when a flexible glycine-serine G
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