Figure 1.
Identification of heavy chain-only domains that interact with human β-Klotho. A, schematic representation of the structures of VHO, HCAb, and a traditional IgG antibody. B, binding of VHO1 and 2 to human β-Klotho measured by bio-layer interferometry. KD values were estimated using a globally fitted 1:1 binding model. Data are mean ± S.E. (n = 3). C, binding of VHO1 and 2 (30 nm) to human FGFR1c measured by bio-layer interferometry. D, competition between VHO2 and VHO1 for β-Klotho binding. Human β-Klotho ECD His6 protein was immobilized onto biosensors in an Octet RED instrument and exposed to VHO1 and VHO2 (30 nm) in two consecutive association steps. E, competition between VHOs and FGF21 for β-Klotho binding. Human β-Klotho ECD His6 protein was immobilized onto biosensors in an Octet RED instrument and exposed to FGF21 (30 nm) and VHO1 or 2 (30 nm) in two consecutive association steps. Data are representative of three independent experiments.