ArticleProtein science : a publication of the Protein Society2004
Affinity transfer by CDR grafting on a nonimmunoglobulin scaffold.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 54 citations in OpenAlex.
- Computational refinement and multivalent engineering of complementarity-determining region-grafted nanobodies on a humanized scaffold for retaining antiviral efficacy.Briefings in bioinformatics · 2025Article
- In silico designing and optimization of anti-epidermal growth factor receptor scaffolds by complementary-determining regions-grafting technique.Quantitative biology (Beijing, China) · 2024Article
- DNA Framework Programmed Conformational Reconstruction of Antibody Complementary Determining Region.JACS Au · 2023Article
- Ultrahigh specificity in a network of computationally designed protein-interaction pairs.Nature communications · 2018Article
- Artificial antibody created by conformational reconstruction of the complementary-determining region on gold nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Many Routes to an Antibody Heavy-Chain CDR3: Necessary, Yet Insufficient, for Specific Binding.Frontiers in immunology · 2018Article
- Circumventing the stability-function trade-off in an engineered FN3 domain.Protein engineering, design & selection : PEDS · 2016Article
- Deep sequencing in library selection projects: what insight does it bring?Current opinion in structural biology · 2015Review
- Functional consequences of complementarity-determining region deactivation in a multifunctional anti-nucleic acid antibody.The Journal of biological chemistry · 2013Article
- Using phage display selected antibodies to dissect microbiomes for complete de novo genome sequencing of low abundance microbes.BMC microbiology · 2013Article
- Evaluating the use of Apo-neocarzinostatin as a cell penetrating protein.Protein engineering, design & selection : PEDS · 2013Article
- Contributions of the complementarity determining regions to the thermal stability of a single-domain antibody.PloS one · 2013Article
- Using microdialysis to analyse the passage of monovalent nanobodies through the blood-brain barrier.British journal of pharmacology · 2012Article
- Antiviral activity of recombinant ankyrin targeted to the capsid domain of HIV-1 Gag polyprotein.Retrovirology · 2012Article
- Affinity transfer to a human protein by CDR3 grafting of camelid VHH.Protein science : a publication of the Protein Society · 2011Article
- Investigating the properties of Bacillus thuringiensis Cry proteins with novel loop replacements created using combinatorial molecular biology.Applied and environmental microbiology · 2008Article
- Antibody binding loop insertions as diversity elements.Nucleic acids research · 2006Article
- A new generation of protein display scaffolds for molecular recognition.Protein science : a publication of the Protein Society · 2006Review
- The antibody mining toolbox: an open source tool for the rapid analysis of antibody repertoires.mAbsArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neocarzinostatin (NCS) is a small "all beta" protein displaying the same overall fold as immunoglobulins. This protein possesses a well-defined hydrophobic core and two loops structurally equivalent to the CDR1 and CDR3 of immunoglobulins. NCS is the most studied member of the enediynechromoprotein family, and is clinically used as an antitumoral agent. NCS has promise as a drug delivery vehicle if new binding specificities could be conferred on its protein scaffold. Previous studies have shown that the binding specificity of the crevasse can be extended to compounds completely unrelated to the natural enediyne chromophore family. We show here that it is possible to introduce new interaction capacities to obtain a protein useful for drug targeting by modifying the immunoglobulin CDR-like loops. We transferred the CDR3 of the VHH chain of camel antilysozyme immunoglobulin to the equivalent site in the corresponding loop of neocarzinostatin. We then evaluated the stability of the resulting structure and its affinity for lysozyme. The engineered NCS-CDR3 presents a structure similar to that of the wild-type NCS, and is stable and efficiently produced. ELISA, ITC, and SPR measurements demonstrated that the new NCS-CDR3 specifically bound lysozyme.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.