. 2022 Aug 10;11(8):1085. doi: 10.3390/antibiotics11081085

Table 1.

Physical parameters and the minimal inhibitory concentration (µg/mL) of designed peptides against E. faecium.

Peptide	Sequence ^a	NC ^b	Hph% ^c	Hy ^d	Hm ^e	rT ^f (min)	MIC (µg/mL)
Peptide	Sequence ^a	NC ^b	Hph% ^c	Hy ^d	Hm ^e		EF C68 ^g
1L	RRWQWRLLLL-NH₂	3	60	0.805	0.168	18.083	16
2L	RRWLWRL-NH₂	3	57	NP	NP	13.321	>32
3L	LRWLWRRRWLWR-NH₂	5	58	0.754	0.146	16.145	16
4L	RLWLWRRRWLWR-NH₂	5	58	0.754	0.219	18.377	4
5L	RRWLWLRRWLWR-NH₂	5	58	0.754	0.333	17.522	4
6L	RRWLWRLRWLWR-NH₂	5	58	0.754	0.425	18.603	4
7L	RRWLWRRLWLWR-NH₂	5	58	0.754	0.214	16.290	4
8L	RRWLWRRRWLWL-NH₂	5	58	0.754	0.075	21.235	4
Amp	N.P.	N.P.	N.P.	N.P.	N.P.	N.P.	>32
Van	N.P.	N.P.	N.P.	N.P.	N.P.	N.P.	>32

^a Peptide sequences have free N-terminus and amidated at C-terminus; ^b NC denotes net charge; ^c Hph% represents the hydrophobic amino acid compositions (total hydrophobic ratio) in the peptide; ^d Hy: Hydrophobicity and ^e Hm: hydrophobic moment of respective peptides calculated from HeliQuest analysis (https://heliquest.ipmc.cnrs.fr/, accessed on 20 June 2022); N.P. is Not predictable by the HeliQuest software; ^f HPLC retention time in mins on a C18 reverse-phase column; ^g E. faecium strain C68 is ampicillin (Amp) and vancomycin (Van) resistant [40].