Centre for Oncology, Radiopharmaceuticals and Research, Biologics and Radiotherapeutic Drugs Directorate, Health Canada, 251 Sir Frederick Banting Driveway, Ottawa, ON, K1A 0K9, Canada.
Department of Chemistry, Carleton University, Ottawa, ON, K1S 5B6, Canada.
Biomol NMR Assign. 2022 Oct;16(2):391-398. doi: 10.1007/s12104-022-10109-z. Epub 2022 Sep 9.
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.
单克隆抗体（mAbs）治疗药物是最大和增长最快的生物药物类别，其中绝大多数是免疫球蛋白 G1（IgG1）。它们的抗原结合能力被用于治疗免疫性疾病、癌症治疗、药物作用逆转以及靶向病毒和细菌。治疗性 mAbs 及其衍生物的重要性很高，因此需要为方法开发和校准生成特征良好的标准。美国国家标准与技术研究院（NIST）开发的基于抗体 motavizumab 的 NISTmAb RM 8621 就是这样的一种标准。在这里，我们展示了通过连接 NISTmAb 的重链和轻链的可变域而工程化的单链可变片段（NISTmAb-scFv）的共振分配。此外，向 NISTmAb-scFv 样品中添加与 motavizumab 靶抗原相对应的肽，会导致抗原结合界面上的残基发生化学位移扰动，从而表明 NISTmAb-scFv 的正确折叠。
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