ArticleBiomolecular NMR assignments2022
Backbone and side-chain resonance assignments of the NISTmAb-scFv and antigen-binding study.
Article in Biomolecular NMR assignments, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 8 citations in OpenAlex.
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- Toward site-specific characterization of structural perturbations on glycosylated Fc using NMR at natural abundance.Journal of biomolecular NMR · 2026Article
- A fast and efficient strategy for the NMR assignment of Fab methyl groups.Journal of biomolecular NMR · 2026Article
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4 authors at 2 institutions in 1 country.
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Abstract
Monoclonal antibodies (mAbs) therapeutics are the largest and fastest growing class of biologic drugs, amongst which, the vast majority are immunoglobulin G1 (IgG1). Their antigen binding abilities are used for the treatment of immunologic diseases, cancer therapy, reversal of drug effects, and targeting viruses and bacteria. The high importance of therapeutic mAbs and their derivatives has called for the generation of well-characterized standards for method development and calibration. One such standard, the NISTmAb RM 8621 based on the antibody motavizumab, has been developed by the National Institute of Standards and Technologies (NIST) in the US. Here, we present the resonance assignment of the single chain variable fragment, NISTmAb-scFv, that was engineered by linking the variable domains of the heavy and light chains of the NISTmAb. Also, addition of a peptide, corresponding to the target antigen of motavizumab, to samples of NISTmAb-scFv has induced chemical shift perturbations on residues lining the antigen binding interface thereby indicating proper folding of the NISTmAb-scFv.
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