期刊
CHEMICAL SCIENCE
卷 13, 期 22, 页码 6610-6618出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d2sc01536f
关键词
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资金
- National Institutes of Health [R01AI148419, R01AI125337, R21AI159203]
- Robert A. Welch Foundation [F-1155]
- National Cancer Institute of the National Institutes of Health [F31CA257404]
This study applied UVPD to probe the paratopes of nanobodies and successfully located the antigen binding sites and intermolecular salt-bridges. This expands the capabilities of UVPD as a new strategy for characterization of nanobodies.
Following immense growth and maturity of the field in the past decade, native mass spectrometry has garnered widespread adoption for the structural characterization of macromolecular complexes. Routine analysis of biotherapeutics by this technique has become commonplace to assist in the development and quality control of immunoglobulin antibodies. Concurrently, 193 nm ultraviolet photodissociation (UVPD) has been developed as a structurally sensitive ion activation technique capable of interrogating protein conformational changes. Here, UVPD was applied to probe the paratopes of nanobodies, a class of single-domain antibodies with an expansive set of applications spanning affinity reagents, molecular imaging, and biotherapeutics. Comparing UVPD sequence fragments for the free nanobodies versus nanobody center dot antigen complexes empowered assignment of nanobody paratopes and intermolecular salt-bridges, elevating the capabilities of UVPD as a new strategy for characterization of nanobodies.
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