ArticleScientific reports2024
Development of novel humanized VHH synthetic libraries based on physicochemical analyses.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Efficient generation of epitope-targeted antibodies with Germinal.Nature biotechnology · 2026Article
- Development of an inhibitory monoclonal nanobody targeting Streptococcus pyogenes siderophore binding protein FtsB.The Journal of biological chemistry · 2026Article
- Discovering Novel Therapeutic VbioRxiv : the preprint server for biology · 2026Article
- Discovering novel therapeutic VFrontiers in immunology · 2026Article
- Article
- J3ExoA: A Novel Anti-HIV Immunotoxin Fusion of Anti-Gp120 J3VHH and PE38 Fragment ofPharmaceuticals (Basel, Switzerland) · 2025Article
- Targeting CD155 in lung adenocarcinoma: A5 nanobody-based therapeutics for precision treatment and enhanced drug delivery.Signal transduction and targeted therapy · 2025Article
- PRELP functions via multiple interactions with intrinsically weak affinity relying on ECM anchoring and remodeling.Scientific reports · 2025Article
- Affinity-stability trade-off mechanism of residue 35 in framework region 2 of VProtein science : a publication of the Protein Society · 2025Article
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Authors and funding
3 authors.
Funding
Abstract
Due to the high affinity and specificity of antibodies toward antigens, various antibody-based applications have been developed. Recently, variable antigen-binding domains of heavy-chain antibodies (VHH) have become an attractive alternative to conventional fragment antibodies due to their unique molecular characteristics. As an antibody-generating strategy, synthetic VHH libraries (including humanized VHH libraries) have been developed using distinct strategies to constrain the diversity of amino acid sequences. In this study, we designed and constructed several novel synthetic humanized VHH libraries based on biophysical analyses conducted using the complementarity determining region-grafting method and comprehensive sequence analyses of VHHs deposited in the protein data bank. We obtained VHHs from the libraries, and hit clones exhibited considerable thermal stability. We also found that VHHs from distinct libraries tended to have different epitopes. Based on our results, we propose a strategy for generating humanized VHHs with distinct epitopes toward various antigens by utilizing our library combinations.
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