Title : Characterization and analysis of scFv-IgG bispecific antibody size variants.

Pub. Date : 2018 Nov-Dec

PMID : 30130449






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 To improve biochemical stability, cysteine residues are often engineered on the heavy- and light-chain regions of the scFv to form an intrachain disulfide bond. Cysteine immunglobulin heavy chain variable region Homo sapiens
2 Structural characterization studies showed that the size variants resulted from the engineered disulfide bond on the scFv, whereby the engineered disulfide was found to be either open or unable to form an intrachain disulfide bond due to cysteinylation or glutathionylation of the cysteines. Cysteine immunglobulin heavy chain variable region Homo sapiens
3 Furthermore, the scFv engineered cysteines also formed intermolecular disulfide bonds, leading to the formation of highly stable dimers and aggregates. Cysteine immunglobulin heavy chain variable region Homo sapiens