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[Preprint]. 2024 Jan 27:2024.01.26.577394. [Version 1] doi: 10.1101/2024.01.26.577394

Table 2.

Binding characteristics of IPI anti-integrin antibodies.

Antibody (Motif in CDR3) Antigen IgG cell surface immunostaining EC50 (nM) IgG ectodomain SPR Kd (nM) IgG competition of ectodomain binding to RGD mimetic Kd (nM) IgG binding to ligand binding site on cell surface Kd (nM) Fab binding to ligand binding site on cell surface KD (nM) IgG inhibition of cell adhesion IC50 (nM)
IPI-αVβ3.7 (RGD) αVβ3 3.7 ± 0.1 0.39 ± 0.08 0.76 ± 0.02 1.09 ± 0.46 12.0 ± 1.8 42.6 ± 9.1
αVβ8 - - 2200 ± 800 - n.d. -
IPI-αVβ3.13 (RLD) αVβ3 2.3 ± 0.4 1.2 ± 0.1 2.6 ± 0.9 1.35 ± 0.36 38.8 ± 5.9 26.6 ± 4.9
IPI-αVβ5.9 (RGD) αVβ5 0.76 ± 0.13 4.8 ± 0.4 2.4 ± 0.7 0.74 ± 0.28 41.9 ± 6.3 5.0 ± 0.1
αVβ3 - 490.5 ± 17.2 1700 ± 400 1200 ± 400 n.d. -
αVβ8 - - - 5200 ± 100 n.d. -
IPI-αVβ6.3 (RGD) αVβ6 5.0 ± 2.0 2.3 ± 0.6 5.5 ± 0.5 0.99 ± 0.20 50.8 ± 4.8 2100 ± 500
αVβ8 - - - - n.d. -
IPI-αVβ6.4 (RTD) αVβ6 5.7 ± 2.9 10.4 ± 4.7 2.2 ± 0.2 0.73 ± 0.14 60.9 ± 5.8 7400 ± 2800
αVβ8 7.2 ± 2.1 18.9 ± 7.1 11.3 ± 2.2 2.66 ± 0.41 131.2 ± 11.2 5.1 ± 1.1
αVβ1 - - 2400 ± 700 - n.d. -
IPI-αVβ6.12 (RGD) αVβ6 3.4 ± 1.6 2.2 ± 0.2 2.3 ± 0.3 1.08 ± 0.21 24.0 ± 2.3 1900 ± 400
αVβ8 - 386.9 ± 34.6 630 ± 140 - n.d. -
αVβ1 - n.r.f. 2800 ± 800 - n.d. -
αVβ3 - - 2300 ± 600 - n.d. -
IPI-αVβ6.2 αVβ6 3.4 ± 1.2 11.3 ± 0.5 n.a. n.a. n.a. 3700 ± 700
αVβ8 - 172 ± 36 n.a. n.a. n.a.
αVβ1 - n.r.f. n.a. n.a. n.a. -
IPI-αVβ8.1 αVβ8 2.6 ± 0.6 0.27 ± 0.16 n.a. n.a. n.a. -
IPI-αVβ8.8 αVβ8 0.69 ± 0.20 1.6 ± 0.7 n.a. n.a. n.a. -
IPI-α5β1.2 α5β1 0.22 ± 0.05 1.9 ± 0.2 n.a. n.a. n.a. -
IPI-α5β1.4 α5β1 0.17 ± 0.06 4.3 ± 0.1 n.a. n.a. n.a. -
αVβ6 - n.r.f. n.a. n.a. n.a. -

Results in columns 1 – 6 are averages ± s.d. from Figs. 2; 3 and S. Fig 14; 4; 5 and 6 IgG data; 6; and 7 respectively.

n.a.: not applicable.

n.d.: not done.

-: no binding/inhibition.

n.r.f.: no reliable fit.