. 2016 Jan 30;173(5):826–838. doi: 10.1111/bph.13384

Table 1.

Affinity and inhibitory potencies of the GIP variants

	Competitive binding				cAMP accumulation
	logIC₅₀ ± SEM	K_i (nM)	Fold	n	logIC₅₀ ± SEM	IC₅₀ (nM)	n
GIP(1–30)NH₂	−9.05 ± 0.02	0.89	1.0	13	—	—	—
GIP(2–30)NH₂	−7.85 ± 0.04	14.3	16	10	−7.66 ± 0.1	21.7	4
GIP(3–30)NH₂	−8.63 ± 0.04	2.3	2.6	12	−7.93 ± 0.04	11.8	6
GIP(4–30)NH₂	−7.67 ± 0.02	21.5	24	3	−6.97 ± 0.4	108	4
GIP(5–30)NH₂	−8.23 ± 0.05	5.9	6.6	3	−7.92 ± 0.4	11.9	4
GIP(6–30)NH₂	−6.46 ± 0.09	347	391	10	−6.47 ± 0.6	342	4
GIP(7–30)NH₂	−7.58 ± 0.08	26	30	9	−6.86 ± 0.4	137	7
GIP(8–30)NH₂	−7.10 ± 0.04	79	89	3	−6.88 ± 0.5	133	5
GIP(9–30)NH₂	−6.51 ± 0.08	307	345	3	−6.35 ± 0.6	450	4

The data shown are the IC₅₀ values from the binding studies (Figure 2) with the fold change relative to the affinity of GIP(1‐30)NH₂ and the cAMP accumulation studies (Figure 3) with antagonist properties.