A bispecific immunotweezer prevents soluble PrP oligomers and abolishes prion toxicity
Fig 3
The bispecific antibody scPOM-bi binds simultaneously to GD and FT of PrP with high affinity.
SPR sensorgrams for binding of scPOM-bi to truncated PrP constructs lacking FT (A) or GD (B) indicate that both antigen binding sites of scPOM-bi correctly engage their target. The bispecific antibody (E) had a stronger affinity than its individual components (C-D) due to avidity resulting in a slower dissociation. The fitting of the experimental data used to calculate the binding constants is in grey. Values for the above plus the full IgG versions of POM1 and POM2 are summarized in (F).