Table 2. Synthetic chemerin peptides¹.

Name	sequence	H	rHMβ	rHMα	ratio	netchg
p1	ELTEAQRRGLQVALEEFHKH	−2.40	0.124	0.466	0.27	0.1
p2	EFHKHPPVQWAFQETSVESA	−1.58	0.169	0.204	0.83	−0.9
p3	SVESAVDTPFPAGIFVRLEF	0.42	0.247	0.109	2.27	−2.0
p4	VRLEFKLQQTSCRKRDWKKP	−3.28	0.375	0.157	2.40	5.0
p5	DWKKPECKVRPNGRKRKCLA	−4.41	0.295	0.205	1.44	6.0
p6	RKCLACIKLGSEDKVLGRLV	−1.27	0.170	0.119	1.43	3.0
p7	LGRLVHCPIETQVLREAEEH	−1.53	0.095	0.080	1.18	−0.9
p8	EAEEHQETQCLRVQRAGEDP	−4.44	0.244	0.177	1.38	−3.4
p9	DPHSFYFPGQFAFSKELPRS	−0.56	0.205	0.250	0.82	0.5
p10	VQRAGEDPHSFYFPGQFAFS	−0.59	0.223	0.186	1.20	−0.5
p11	QVLREAEEHQETQCLRVQRA	−3.58	0.141	0.278	0.51	−0.4
p12	NGRKRKCLACIKLGSEDKVL	−2.81	0.284	0.046	6.20	4.0
p13	NGRKRKCLACIKLGSEDKVLGRLVH	−2.34	0.168	0.167	1.00	5.5
p14	KALPRS	−2.63	0.100	0.609	0.16	2.0
pg-1	RGGRLCYCRRRFCVCVGR	−2.56	0.376	0.227	1.66	6.0
mag-2	GIGKFLHSAKKFGKAFVGEIMNS	−0.58	0.104	0.505	0.21	3.5

Peptide 4 is shown in bold. The net charge at pH 6 (netchg), mean hydrophobicity (H), relative mean hydrophobic moment assuming a β structure and α-helix, (rHMβ) and (rHMα) respectively, and rHMβ/rHMα ratio are indicated for each peptide. Data for the antibacterial peptide protegrin-1 (pg-1) and magainin-2 (Mag-2) known to adopt β structure and α-helical conformation, respectively when bound to the lipid membrane [36], [37], are shown for comparison. The rHM values and rHMβ/rHMα ratio for preferred peptide conformation are shown in bold.

¹chemerin peptides-patent pending.