TABLE 2 

Inhibition of WT-RGS: Gαo interaction/ by RGS inhibitors

Biochemical characterization of RGS inhibitors for their ability to disrupt the WT-RGS: Gαο PPI using AlphaScreen assay. Data represent the IC50 with the 95% CI in parentheses from n = 3 independent experiments, with the average of duplicate wells. Concentration response curves for each value given are shown in Supplemental Fig. S2. NC indicates that an IC50 value was not calculable, due to an altogether lack of inhibition.

RGSIC50, μM
177723319116696383479CCG-63808CCG-559195428579CCG-4986CCG-50014CCG-638021472216UI-5UI-1590
116 (12 to 21)62 (31 to >100)90 (58 to >100)37 (28–51)18 (10–34)18 (13–25)38 (30–50)0.12 (0.10–0.14)23 (19–29)24 (18–33)20 (17–24)1.8 (1.3–2.4)
417 (13–24)82 (46 to >100)7.4 (5.6–9.7)15 (10–23)0.97 (0.58–1.6)9.9 (7.6–13)3.4 (2.4–4.9)0.029 (0.023–0.038)19 (15–25)31 (21–50)15 (9.7–25)1.2 (0.80–1.7)
5>100>100>100>10017 (10–30)58 (31 to >100)50 (37–72)0.6 (0.46–0.80)>10070 (35 to >100)>10018 (12–28)
6NC>100>100NC>100>100>100>100NC>100>100>100
7NC>100>100>100>100>100>100>100>100>100>100>100
840 (30–57)76 (49 to >100)50 (35–78)59 (43–89)16 (11–25)12 (9.2–15)61 (45–90)0.65 (0.29–1.5)44 (34–58)92 (68 to >100)80 (55 to >100)6.4 (5.4–7.7)
10>100>100>100>10068 (46 to >100)>100>1007.6 (6.1–9.6)>100>100>10051 (41–65)
145.0 (4.2–5.9)7.5 (6.0–9.3)>10013 (11–15)2.4 (1.9–3.1)5.9 (5.2–6.7)22 (19–27)0.008 (0.006–0.010)11 (9.3–13)3.2 (2.6–3.9)1.5 (1.3–1.8)0.46 (0.39–0.54)
1676 (56 to >100)>10056 (36 to >100)88 (62 to >100)13 (10–17)51 (34–84)54 (43–70)0.44 (0.30–0.65)62 (46–92)>100>10021 (15–30)
1728 (16–57)>100>100>10011 (7.7–17)41 (31–56)71 (50 to >100)0.78 (0.58–1.0)>10022 (14–36)86 (49 to >100)a7.3 (5.6–9.7)a
18>100>100>100>100>100>100>10028 (14–67)>100>100NC>100
  • a Data previously reported in Bodle et al., 2017b.