Table 1.

Self-assembling synthetic peptides used in this study

Peptide No.	Sequence	n	X	Π∗	Mass (Da)	Charge (at pH 7)†	Charge/mass
Cationic Kn(XKXE)2 peptides
1	Ac-K2(FKFE)2-NH2	2	Phe	1.79	1419	+2.00	1.41 × 10−3
2	Ac-K4(FKFE)2-NH2	4	Phe	1.79	1675	+4.00	2.39 × 10−3
3	Ac-K2(ChaKChaE)2-NH2	2	Cha	2.72	1443	+2.00	1.39 × 10−3
4	Ac-K4(ChaKChaE)2-NH2	4	Cha	2.72	1658	+4.00	2.41 × 10−3
5	Ac-K2(AKAE)2-NH2	2	Ala	0.31	1114	+2.00	1.80 × 10−3
Anionic En(XKXE)2 peptides
6	Ac-E2(FKFE)2-NH2	2	Phe	1.79	1421	−2.00	1.41 × 10−3
7	Ac-E4(FKFE)2-NH2	4	Phe	1.79	1679	−4.00	2.38 × 10−3
8	Ac-E2(ChaKChaE)2-NH2	2	Cha	2.72	1445	−2.00	1.38 × 10−3
9	Ac-E4(ChaKChaE)2-NH2	4	Cha	2.72	1703	−4.00	2.35 × 10−3
SEVI-forming peptide
10	PAP(248–286)	NA	NA	NA	4549	+6.46	1.42 × 10−3

^∗Hydrophobicities based upon the water-octanol partition coefficient relative to glycine (14).

^†MarvinSketch was used to determine charge at pH by calculating the pI of the peptide (33).