Optimization of Disulfide Linkages in Bispecific Antibodies
Disulfide linkages in the complex cysteine-engineered stapled scFv for bispecific antibodies are optimized and characterized.
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Multispecific antibodies are the next generation of biotherapeutics. Their single-chain fragment variable (scFv) domains composed of variable light chain (VL) and heavy chain (VH) are critical and known to have a lower stability and a tendency to aggregate. • We (mAbs. 2023) revealed a stapling strategy by introducing two engineered disulfide bonds between VL and VH domains. The stapled scFv (called spFv) technology for bispecific achieves higher thermal stability and minimal aggregation.
