TABLE 1.

Inhibition constants for cyclic peptides of different lengths in enzymatic assays against DENV3 NS3/2B protease^a

Peptide	Amino acid														Ki (μM)	Fold change
	P3	P2	P1	P1′	P2′	P3′	P4′			35	36	37	38	39
CP1	P	C*	K	A	R	I	I	G	G	Y	G	G	C*	R	232.3 ± 69.9	1.00
CP2	P	C*	K	A	R	I	I	G	G	Y	G	G	C*	A	678.3 ± 244.1	2.92
CP3	P	C*	K	A	R	I		G		Y	G	G	C*	A	376.8 ± 204.1	1.62
CP4	P	C*	R	A	R	I		G		Y	G	G	C*	A	966.1 ± 328.8	4.16
CP5	P	C*	K	A	R	I				Y	G	G	C*	A	14.5 ± 6.7	0.06
CP6	P	C*	R	A	R	I				Y	G	G	C*	R	187.3 ± 43.2	0.81
CP7	P	C*	R	A	R	I				Y	G	G	C*	A	2.9 ± 0.8	0.01
CP8	P	C*	R	A	R	I				Y		G	C*	A	467.9 ± 68.7	2.01
CP9	P	C*	R	A	R	I					G	G	C*	A	780.3 ± 195.5	3.36
CP10	P	C*	R	A	R	I					G	G	C*	R	29.7 ± 5.8	0.13
CP11		C*	R	A	R	I				Y	G	G	C*	R	145.1 ± 27.9	0.62
CP12	P	C*	R	A	R	I						G	C*	A	101.2 ± 24.8	0.44

^aThe amino acid sequence is given based on corresponding substrate positions (P3 to P4′; aprotinin residues 12 to 18) and the linked aprotinin second-loop residue numbers (35 to 39). The peptides were cyclized through a disulfide bond between cysteine residues indicated by an asterisk. The fold changes are relative to CP1.