ArticleProtein science : a publication of the Protein Society2021
Biochemistry, structure, and cellular internalization of a four nanobody-bearing Fc dimer.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 4 citations in OpenAlex.
- Research Progress on the Application of Neutralizing Nanobodies in the Prevention and Treatment of Viral Infections.Microorganisms · 2025Review
- Biochemistry, structure, and cellular internalization of a four nanobody-bearing Fc dimer.Protein science : a publication of the Protein Society · 2021Article
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11 authors at 4 institutions in 2 countries.
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Abstract
VHH stands for the variable regions of heavy chain only of camelid IgGs. The VHH family forms a set of interesting proteins derived from antibodies that maintain their capacity to recognize the antigen, despite their relatively small molecular weight (in the 12,000 Da range). Continuing our exploration of the possibilities of those molecules, we chose to design alternative molecules with maintained antigen recognition, but enhanced capacity, by fusing four VHH with one Fc, the fragment crystallizable region of antibodies. In doing so, we aimed at having a molecule with superior quantitative antigen recognition (×4) while maintaining its size below the 110 kDa. In the present paper, we described the building of those molecules that we coined VHH
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