. Author manuscript; available in PMC: 2019 Jan 25.

Published in final edited form as: Cell. 2018 Jan 4;172(3):618–628.e13. doi: 10.1016/j.cell.2017.12.009

Table 2.

Fold change (log2) and antimicrobial (MBC) activities of peptides from SLAY.

Peptide	Sequence	Group^a	Charge	Hydrophobicity	log2 fold	p-value	MBC (μM)^b

							W3110	Ab5075	PA14	NDM E. coli
Cecropin P1	SWLSKTAKKLENSAKKRISEGIAIAIQGGPR	-	5.000	−0.590	-	-	≤2	≤2	≤2	≤2
P1	RLVRILVSKRPVAIKPYFRL	29	5.997	0.325	−1.98	<1.3e-5	2	≤2	≤2	≤2
P2	TTSIRRRYQVSLIRRHRGKR	67	8.088	−1.490	−3.33	<5.2e-21	16	≤2	≤2	4
P3 cyclic^c	TCRTNRPCFYDLDLNVCRCS	26	0.750	−0.381	−4.60	<2.85e-27	≤2	4	≤2	4
P4	SNGDGTLDAGSTCAPFYARA	49	−1.064	−0.290	−1.63	<8.7e-11	2	16	4	4
P5 cyclic^d	YYNPLPHDCGRDNNTDICSR	46	−1.04	−1.31	−2.88	<8.4 e-34	4	8	≤2	≤2
P6	LSVDKRPVLHPEHIYGHNHY	73	0.362	−0.910	−3.63	<1.2e-51	4	32	8	>128
P7	IHRDQQHESFLDARPEPGLTE	2	−2.814	−1.348	−2.09	<1.4e-9	4	16	4	4
P8	TIDFGVRNINQSNLVYDTER	33	−1.000	−0.670	−2.76	<5.1e-44	8	16	8	>128
P9	PCNPDHDYRPFGNFRIAFTT	60	0.027	−0.845	−2.59	<2.5e-15	8	16	8	8
P10	TRDTNDLISSRTAAPSMV	60	−0.001	−0.422	−10.7	<2.0e-66	16	64	8	32
P11	LPLPSCSSHGGDADNTSQRN	8	−0.972	−1.060	−4.66	<8.5e-59	16	128	16	32
P12	PNDPDSPCVYRMPNARGCSI	75	−0.126	−0.765	−3.80	<2.3e-27	16	128	16	16
P13	YDLSDSNCLPANRDKRYYVI	79	−0.066	−0.845	−1.10	<1.6e-12	16	>128	16	>128
P14	SMLAYVDKNDHINPPHSPRS	10	0.180	−1.055	−5.49	<8.9e-60	32	128	32	64
P15	DATPHAALFFTVKDHTAGDN	69	−1.819	−0.380	−2.83	<8.6e-11	32	64	32	64
P16	SDDAQRCYPHNRTPFTYTYI	39	0.025	−1.230	−2.18	<2.8e-07	32	>128	16	32
P17	EPCSPKNNYHDLFYRT	22	0.027	−1.488	−1.80	<6.2e-6	128	>128	128	>128
P18	CNPLNGADRRTDSFPRFTVI	51	0.937	−0.545	−1.11	<5.2e-8	128	>128	64	>128
P3	TCRTNRPCFYDLDLNVCRCS	26	0.750	−0.400	−4.60	<2.85e-27	>128	128	>128	>128
P5	YYNPLPHDCGRDNNTDICSR	46	−1.035	−1.380	−2.88	<8.4 e-34	>128	>128	128	>128
C1	PDRAIDTYRTSPVADQRYNA	-	−0.002	−1.245	0.09	0.999	>128	>128	>128	>128

Peptide group numbers were determined based on clustering as described in the methods.

Minimal bactericidal concentrations (MBC) were determined as the lowest concentration of peptide that results in at least 99.9% killing of the initial inoculums. Data are representative of three independent experiments.

P3 peptide was synthesized into cyclic formation by two disulfide bonds at C2–C19 and C8–C17.

P5 peptide was synthesized into cyclic formation by one disulfide bond at C9–C18. Disulfide bonds in P3 and P5 are represented by black bars.