From Protein / Ligand Screening to Therapeutic Protein Characterization
8:00 a.m. PDT / 11:00 a.m. EDT / 15:00 GMT
Postdoctoral Research Fellow,
UCB (Slough, UK)
Hubert Curien Pluridisciplinary Institute (CNRS)
This webinar, in two parts, will cover biopharmaceutical applications of native MS for the determination of diverse characteristics including ligand-binding, non-covalent protein interactions, and intact antibody characterization.
In the first part, Rebecca Burnley will address application of native MS to protein-ligand screening. Topics will include how proper desolvation and high spectral resolution allows more reliable measurement of binding, including weak binding and binding of low MW compounds, analysis of heterogenous proteins, and the capability to screen multiple compounds at once.
In the second part, Sarah Cianfé́rani will focus on the possibilities and limitations of native MS in the characterization of monoclonal antibodies (mAbs) and antibody-drug conjugates (ADCs), determining such critical characteristics as drug to antibody ratio (DAR), mAb/ antigen noncovalent complexes characterization, higher order structure determination, and mAbs mixture analysis.
- What is native MS and how can it be useful in drug discovery processe?
- What is the classical native MS-based workflow for protein/ligand and biopharmaceuticals characterization?
- Why use native MS for protein/ligand interaction characterization?
- Why use native MS for therapeutic protein characterization?
- What are the benefits of high resolution native MS for biopharmaceutical characterization?