Table 2.

Sequences of Second Generation Peptides Using Orn, Dab, and Dap and Their K_d Values against IRES^a

peptide	sequencesb	helicity(%)c	Kd [nM]d,e
2a	LKKLLOrnLLKKLLKLAG	13/82	6.1 ± 0.3 (2.5)
2b	LKKLLDabLLKKLLKLAG	23/63	1.6 ± 0.2 (6.3)
2c	LKKLLDapLLKKLLKLAG	26/61	3.8 ± 0.2 (2.4)
2d	LKKLLKLLOrnKLLKLAG	28/57	1.3 ± 0.2 (9.1)
2e	LKKLLKLLDabKLLKLAG	43/57	3.5 ± 0.2 (6.5)
2f	LKKLLKLLDapKLLKLAG	25/57	20 ± 1 (0.6)
2g	LKKLLKLLKKLLOrnLAG	36/53	4.4 ± 0.5 (3.3)
2h	LKKLLKLLKKLLDabLAG	24/34	8.7 ± 0.3 (2.0)
2i	LKKLLKLLKKLLDapLAG	39/54	1.4 ± 0.2 (12)
2j	LKKLLDabLLOrnKLLKLAG	49/57	2.4 ± 0.3 (6.3)
2k	LKKLLKLLOrnKLLDapLAG	48/61	0.68 ± 0.06 (25)
2l	LKKLLDabLLKKLLDapLAG	40/50	1.1 ± 0.1 (13)
2m	LKKLLDabLLOrnKLLDapLAG	49/69	4.3 ± 0.2 (4.9)

^aAffinities were measured at 20 °C using a fluorescence anisotropic technique and rhodamine-Rev peptide as a probe.

^bOrn = Ornithine, Dab = 1,4-diaminobutyric acid, Dap = 1,3-diaminopropionic acid.

^cα-Helicities of peptides alone were measured in 10 mM H₃PO₄ (first value) and in 50% TFE in the same buffer (second value).

^dDiscrimination ratios²⁴ against IRES RNA are written in parentheses.

^eMeasurements of binding affinity were triplicated and averaged.