. Author manuscript; available in PMC: 2024 Jan 23.

Published in final edited form as: Biochemistry. 2023 Mar 27;62(8):1376–1387. doi: 10.1021/acs.biochem.2c00686

Table 1.

Estimated IC₅₀ values from inhibition experiments with 8-azaN duplexes.

8-azaN Duplex	Enzyme	Editing Substrate	IC₅₀ (nM)^†
H₁₆	ADAR1 p110	5-HT_2C	13 ± 2
H₁₆	ADAR1 p110	NEIL1	8.9 ± 0.8
H₁₆	ADAR1 p150	5-HT_2C	28 ± 3
5’−3’ swap	ADAR1 p110	5-HT_2C	15 ± 1
GC-rich	ADAR1 p110	5-HT_2C	18 ± 8
AU-rich	ADAR1 p110	5-HT_2C	74 ± 3
2’-OMe	ADAR1 p110	5-HT_2C	11.4 ± 0.7
H₁₄ A	ADAR1 p110	5-HT_2C	18 ± 4
H₁₄ B	ADAR1 p110	5-HT_2C	> 3000
H₁₂ A	ADAR1 p110	5-HT_2C	> 3000
H₁₂ B	ADAR1 p110	5-HT_2C	> 3000

^†

Data from inhibition experiments were plotted to the equation: y = m1+(m2−m1)/[1+(x/m4)^m3], where y = % editing; x = log of RNA duplex concentration; m1 = basal response; m2 = maximal response; m3 = slope factor or Hill slope; and m4 = log of IC₅₀ value (see Fig. S4 for IC₅₀ plots). Values reported are the average of three independent measurements ± standard deviation.