ArticleMethods in molecular biology (Clifton, N.J.)2012
Expression, purification, and characterization of engineered antibody CH2 and VH domains.
Article in Methods in molecular biology (Clifton, N.J.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- A C-type single-domain antibody with protective efficacy against H1N1 via respiratory administration.Virologica Sinica · 2026Article
- Neutralization of Zika virus by germline-like human monoclonal antibodies targeting cryptic epitopes on envelope domain III.Emerging microbes & infections · 2017Article
- Nanobody-Based Delivery Systems for Diagnosis and Targeted Tumor Therapy.Frontiers in immunology · 2017Review
- Toward a magic or imaginary bullet? Ligands for drug targeting to cancer cells: principles, hopes, and challenges.International journal of nanomedicine · 2015Review
- Interactions of IgG1 CH2 and CH3 Domains with FcRn.Frontiers in immunology · 2014Article
- N-terminal truncation of an isolated human IgG1 CH2 domain significantly increases its stability and aggregation resistance.Molecular pharmaceutics · 2013Article
- Designing and Development of a Tandem Bivalent Nanobody against VEGFAvicenna journal of medical biotechnologyArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Most of the FDA-approved therapeutic monoclonal antibodies are full-size IgG molecules with a molecular weight of about 150 kDa. A major problem for such large molecules is their poor penetration into tissues (e.g., solid tumors) and poor or absent binding to regions on the surface of some molecules (e.g., on the HIV envelope glycoprotein) which are fully accessible only by molecules of smaller size. Therefore, much work especially during the last decade has been aimed at developing novel scaffolds of much smaller size and high stability. Immunoglobulin-based scaffolds including Fab (∼50 kD), ScFv (∼30 kD), and VH domain (termed domain antibody, dAb) (∼15 kD) have been well established. Recently, a new scaffold based on human IgG1 CH2 domain (∼15 kD) was also proposed (termed nanoantibody, nAb). Binders based on a CH2 scaffold could also confer some effector functions. Here, we describe the design, expression, purification, and characterization of engineered CH2 and VH domains.
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