MS Analysis Expert

Read   Effects of Glycosylation on the Stability and Half-life of Antibody Drugs Effects of Glycosylation on the Safety of Antibody Drugs The Critical Quality Attributes   (CQA) of antibody is the standard to judge whether it is qualified. CQA   must be in a proper range to ensure the effectiveness of drugs, and more importantly, the safety of drugs. By affecting the effect function of F c  end, glycosylation modification of F c  end will affect the safety of antibody, which is manifested in immunogenicity, PK/Pd (pharmacokinetics/pharmacodynamics), etc. The development of antibody has experienced mouse antibody, chimeric antibody, humanized antibody, and then to the last all human antibody, throughout which the immunogenicity of antibody has been constantly reduced. For glycosylation , human cells specifically synthesize Neu5Ac sialic acid, while other mammalian cells can not only synthesize Neu5Ac sialic acid, but also synthesize Neu5Gc sialic acid with immunogenicity

Among various post-translational modifications of proteins, glycosylation is one of the most important and complex modifications, and it is also one of the key quality attributes to evaluate antibodies. The realization of the function of monoclonal antibody is closely related to its glycosylation, which will affect the performance of protein, such as conformation, stability, solubility, pharmacokinetics, activity and immunogenicity. Glycosylation is one of the important post-translational modifications of proteins. According to the modified sites of glycosylation, it can be divided into N-glycosylation and O-glycosylation. N-glycosylation is located in asn-297. N-acetylglucosamine in oligosaccharide links itself with  amide nitrogen on asparagine residue  to  modify   protein ,which start s  from endoplasmic reticulum and complete s  in Golgi body .  O-glycosylation is completed in Golgi body by n-acetylgalactose in oligosaccharide linking with hydroxyl on serine or threonine re