Table 3.

Effects of hydrophobic domain on IN inhibition

Compd	R1	linker	R2	R3	IN IC50 (μM)a
					3′P	STb
11c	H	CH2OCH2	iPr	benzyl	>111	21 ± 2
51	H	CH2OCH2	iPr	4-Fbenzyl	>111	7.3 ± 0.8
52	F	CH2OCH2	iPr	4-Fbenzyl	>111	5.5 ± 0.7
53	H	CH2OCH2	Et	benzyl	>111	8.2 ± 1.0
54	H	CH2OCH2	Me	H	>111	75 ± 7
55	H	CH2OCH2	benzyl	Et	>111	36 ± 6
56	F	CH2OCH2	benzyl	Et	>111	11 ± 0.8
64	H	CH2	iPr	4-Fbenzyl	>111	32 ± 6
65	F	CH2	iPr	4-Fbenzyl	>111	73 ± 12
66	H	CH2	iPr	benzyl	>111	28 ± 2
67	H	CH2	Et	benzyl	>111	>111
68	F	CH2	Et	benzyl	>111	24 ± 3
69	H	CH2	Me	H	>111	>111
70	F	CH2	Me	H	>111	>111
75	H	CH2	benzo (fused)		>111	>111
76	F	CH2	benzo (fused)		>111	>111

^aConcentration inhibiting enzymatic function by 50%.

^bMean value ± standard deviation from triplicate experiments.

^cRef ³⁰.