AI Article Synopsis
- Monoclonal antibodies (mAbs) are crucial for developing lifesaving drugs and consist of two main parts: the antigen-binding fragment (Fab) and the crystallizable fragment (Fc).
- Research has faced challenges in getting a fully functional, labeled Fab domain, particularly in the NMR assignment process.
- This study succeeded in producing a triply-labeled Fab domain from the standard IgG1κ (NISTmAb) in yeast, leading to the assignment of 94% of its backbone atoms.
Article Abstract
The monoclonal antibody (mAb) protein class has become a primary therapeutic platform for the production of new life saving drug products. MAbs are comprised of two domains: the antigen-binding fragment (Fab) and crystallizable fragment (Fc). Despite the success in the clinic, NMR assignments of the complete Fab domain have been elusive, in part due to problems in production of properly folded, triply-labeled H,C,N Fab domain. Here, we report the successful recombinant expression of a triply-labeled Fab domain, derived from the standard IgG1κ known as NISTmAb, in yeast. Using the H,C,N Fab domain, we assigned 94% of the H, C, and N backbone atoms.
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| http://dx.doi.org/10.1007/s12104-023-10123-9 | DOI Listing |
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