Physical stability comparisons of IgG1-Fc variants: effects of N-glycosylation site occupancy and Asp/Gln residues at site Asn 297

Alsenaidy MA, et al., doi: 10.1002/jps.23975, J Pharm Sci, 2014

The authors performed structural integrity and conformational stability studies on various IgG1-Fc proteins and mutant forms produced from the yeast Pichia pastoris to better understand the different glycosylation site occupancies and how these modifications regulate the biological activity of mAbs. Binding interactions were studied on the Blitz instrument. Protein G biosensors were used.

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