ArticleProtein science : a publication of the Protein Society2019
VHH characterization. Comparison of recombinant with chemically synthesized anti-HER2 VHH.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation.Military Medical Research · 2026Review
- Enhanced native chemical ligation by peptide conjugation in trifluoroacetic acid.Science advances · 2024Article
- Modulatory actions ofFrontiers in cellular and infection microbiology · 2024Article
- Molecular imaging for better theranostics.European journal of nuclear medicine and molecular imaging · 2023Article
- Serum albumin binding knob domains engineered within a VFrontiers in immunology · 2023Article
- Modular Site-Specific Conjugation of Nanobodies Using Two Co-Associating Tags.International journal of molecular sciences · 2022Article
- Total Chemical Synthesis of a Functionalized GFP Nanobody.Chembiochem : a European journal of chemical biology · 2022Article
- Biochemistry, structure, and cellular internalization of a four nanobody-bearing Fc dimer.Protein science : a publication of the Protein Society · 2021Article
- Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020Review
- VHH characterization. Comparison of recombinant with chemically synthesized anti-HER2 VHH.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
15 authors.
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Abstract
In the continuous exploration of the VHH chemistry, biochemistry and therapeutic future use, we investigated two different production strategies of this small antibody-like protein, using an anti-HER2 VHH as a model. The total chemical synthesis of the 125 amino-acid peptide was performed with reasonable yield, even if optimization will be necessary to upgrade this kind of production. In parallel, we expressed the same sequence in two different hosts: Escherichia coli and Pichia pastoris. Both productions were successful and led to a fair amount of VHHs. The integrity and conformation of the VHH were characterized by complementary mass spectrometry approaches, while surface plasmon resonance experiments were used to assess the VHH recognition capacity and affinity toward its "antigen." Using this combination of orthogonal techniques, it was possible to show that the three VHHs-whether synthetic or recombinant ones-were properly and similarly folded and recognized the "antigen" HER2 with similar affinities, in the nanomolar range. This opens a route toward further exploration of modified VHH with unnatural amino acids and subsequently, VHH-drug conjugates.
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Registered trials
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