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. 2021 Jul 12;9(7):e002444. doi: 10.1136/jitc-2021-002444

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© Author(s) (or their employer(s)) 2021. Re-use permitted under CC BY-NC. No commercial re-use. See rights and permissions. Published by BMJ.

This is an open access article distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited, appropriate credit is given, any changes made indicated, and the use is non-commercial. See http://creativecommons.org/licenses/by-nc/4.0/.

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Biophysical characterization and murine pharmacokinetics of HER-2/CD3 BsAbs. (A) Schematic diagrams of the tandem Fab and IgG BsAbs. The linker between the Fabs within the tandem Fab BsAb comprises a (G₄S)₃ 15 amino acid (aa) sequence. (B) Analytical size-exclusion chromatography of the HER-2/CD3 BsAbs including a tandem scFv (BiTE) BsAb that connected the VH/VL domains of each Fv using a 20 aa (G4S)₃ linker and a 15 aa (G₄S)₃ linker between the Fvs. The tandem scFv was unstable and degraded when expressed multiple times. (C) Intact mass spectra of the HER-2/CD3 IgG (green/above) and tandem Fab (blue/below) BsAbs indicating >95% correct HC/LC assembly. (D) Pharmacokinetic properties of the HER-2/CD3 IgG1AA_N297Q and tandem Fab BsAbs compared with the parental pertuzumab human IgG1 and chimeric SP34 human IgG1AA_N297Q mAbs on intravenous dosing (four mice/group; error bars are shown). BiTE, Bispecific T cell Engager; BsAb, bispecific antibody; mAb, monocolonal antibody; scFv, single-chain variable fragment.