TABLE 2.

Inhibition constants for cyclic peptides with sequence optimization against DENV3 NS3/2B protease^a

Peptide	Amino acid											Ki (μM)	Fold change
	P3	P2	P1	P1′	P2′	P3′	35	36	37	38	39
CP7	P	C*	R	A	R	I	Y	G	G	C*	A	2.9 ± 0.8	1.00
CP13	Bzb	C*	R	A	R	I	Y	G	G	C*	A	33.2 ± 6.5	11.45
CP14	P	C*	R	A	Q	I	Y	G	G	C*	A	NBc	NB
CP15	P	C*	R	A	W	I	Y	G	G	C*	R	19.7 ± 8.8	6.79
CP16	P	C*	R	A	W	I	Y	G	G	C*	A	144.8 ± 54.4	49.93
CP17	P	C*	R	A	R	I	D	G	G	C*	A	69.3 ± 24.4	23.90
CP18	P	C*	R	V	R	I	D	G	G	C*	A	35.8 ± 16.4	12.34
CP19	P	C*	R	V	R	I	Y	G	G	C*	A	25.6 ± 9.9	8.83

^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 CP7.

^bBz denotes benzoyl capping group.

^cNB, no binding.