TY - JOUR
AU - Cymer , Florian
AB - The usefulness of higher-order structural information provided by hydrogen/deuterium exchange-mass spectrometry (H/DX-MS) for the structural impact analyses of chemical and post-translational antibody modifications has been demonstrated in various studies. However, the structure–function assessment for protein drugs in biopharmaceutical research and development is often impeded by the relatively low-abundance (below 5%) of critical quality attributes or by overlapping effects of modifications, such as glycosylation, with chemical amino acid modifications; e.g., oxidation or deamidation. We present results demonstrating the applicability of the H/DX-MS technique to monitor conformational changes of specific Fc glycosylation variants produced by in vitro glyco-engineering technology. A trend towards less H/DX in Fc Cγ2 domain segments correlating with larger glycan structures could be confirmed. Furthermore, significant deuterium uptake differences and corresponding binding properties to Fc receptors (as monitored by SPR) between α-2,3- and α-2,6-sialylated Fc glycosylation variants were verified at sensitive levels.
TI - The Impact of Immunoglobulin G1 Fc Sialylation on Backbone Amide H/D Exchange
JF - Antibodies
DO - 10.3390/antib8040049
DA - 2019-10-01
UR - https://www.deepdyve.com/lp/multidisciplinary-digital-publishing-institute/the-impact-of-immunoglobulin-g1-fc-sialylation-on-backbone-amide-h-d-veWbjT997G
VL - 8
IS - 4
DP - DeepDyve
ER -