Full-length and N-terminally truncated recombinant interleukin-38 variants are similarly inefficient in antagonizing interleukin-36 and interleukin-1 receptors

Table 2 Recombinant IL-38 proteins bind to the IL-36R with moderate affinity

recombinant protein	ka1 (1/Ms)	kd1 (1/s)	ka2 (1/s)	kd2 (1/s)	KD (M)
IL-36Ra	1.29E + 04	2.71E-02	2.82E-03	6.61E-05	4.82E-08
IL-38 2-152His	7.17E + 03	1.48E-02	3.58E-03	6.71E-04	3.25E-07
IL-38 2-152	9.67E + 03	2.26E-02	3.92E-03	7.25E-04	3.66E-07
IL-38 3-152	2.81E + 03	1.63E-02	4.16E-03	9.47E-04	1.08E-06
icIL-1Ra1	9.63E + 03	3.19E-01	5.25E-05	5.38E-02	3.31E-05

Binding of recombinant human IL-36Ra, IL-38 variants (aa 2-152 with C-terminal His tag; aa 2-152; aa3-152) and icIL-1Ra1 to an immobilized IL-36R-Fc chimeric protein was analyzed by SPR using a two-state reaction model. The binding results are reported as association (ka) and dissociation (kd) rate constants and binding affinity (KD)

ISSN: 1478-811X