TABLE 1.

Primary sequence and antipseudomonal activity of full-length peptides^a

Peptide	Peptide sequence	EC50 (μM) against P. aeruginosa PAO1b
		Low salt	High salt
mCRAMP	ISRLAGLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ	0.40 ± 0.05 (7)	1.07 ± 0.16 (6)
rCRAMP	ISRLAGLVRKGGEKFGEKLRKIGQKIKEFFQKLALEIEQ	0.74 ± 0.06 (4)	2.38 ± 0.61 (3)
SMAP34	GLFGRLRDSLQRGGQKILEKAERIWCKIKDIFRG	0.37 ± 0.05 (3)	1.04 ± 0.14 (3)
SMAP29	RGLRRLGRKIAHGVKKYGPTVLRIIRIAG	0.05 ± 0.01 (8)	0.06 ± 0.01 (7)
CAP18	GLRKRLRKFRNKIKEKLKKIGQKIQGLLPKLAPRTDY	0.22 ± 0.05 (6)	0.11 ± 0.02 (4)
FALL39	FALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES	0.52 ± 0.04 (3)	0.73 ± 0.08 (3)
LL37	LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES	0.81 ± 0.13 (3)	1.47 ± 0.33 (3)

^aSequences were aligned with the CLUSTAL program (35). The cationic amino acids arginine (R) and lysine (K) are underlined. Activity was determined by the luminescence assay under low-salt (25 mM NaCl) or high-salt (175 mM NaCl) conditions, as described in Materials and Methods. Calculated molecular weights for the peptides are as follows: mCRAMP, 4,419; rCRAMP, 4,473; SMAP34, 3,988; SMAP29, 3,256; FALL39, 4,711; LL37, 4,493; CAP18, 4,434. 

^bData are mean EC₅₀ ± standard error of the mean, and the number of experiments (n) is indicated.