Table 2.

Characterization of Structural Changes for 14 Peptides in the Presence of DA

Sequence	0 mM DA		4.5 mM DA		18 mM DA			72 mM DA
	Appearance	CD	Appearance	CD	Appearance	CD	ATR-FTIR	Appearance	CD	ATR-FTIR
RFRFRFR-NH2	C	max@ 220 nm	F	max@ 220 nm	F	-	–	F	-	β+
FRFRFR-NH2	C	max@ 220 nm	C	max@ 220 nm	F	-	–	F	max@ 220 nm	–
DFRFRF-NH2	F	max@ 220 nm	F	-	F	-	β+	F	min@ 215 nm	β2+
RFRFDF-NH2	C	max@ 220 nm	C	max@ 220 nm	F	-	β+	T	max@ 220 nm	–
RFRFR-NH2	C	max@ 220 nm	C	max@ 220 nm	T	-	–	F	-	–
RFRFD-NH2	C	max@ 220 nm	C	max@ 220 nm	C	max@ 220 nm	–	NC	max@ 220 nm	–
Ac-VOVAVOVAV-NH2	F	min@ 220 nm	F	min@ 220 nm	F	min@ 220 nm	β2+	F	β	β2+
Ac-V-{Dab}-VAV-{Dab}-VAV-NH2	F	min@ 190–220 nm	F	min@ 197 and 220 nm	F	min@ 197 and 220 nm	β2+	F	β	β2+
VOVOVOVOV-NH2	C	RC	F	RC	F	-	β2+	F	β	β2+
V-{Dab}-V-{Dab}-V-{Dab}-V-{Dab}-V-NH2	F	min@ 220 nm	F	min@ 220 nm	F	-	β2+	F	min@ 220 nm	β2+
V-{Dab}-V-{Dab}-V-{Dab}-V-NH2	C	RC	F	RC	F	-	β+	F	min@ 205 nm	β2+
{Dab}-V-{Dab}-V-{Dab}-V-{Dab}-V-NH2	F	min@ 225 nm	C	min@ 225 nm	F	-	β2+	T	min@ 220 nm	β+
{Dab}-V-{Dab}-V-{Dab}-V-NH2	C	RC	C	RC	F	-	–	T	β	–
(OV)4	C	RC	C	RC	F	-	β2+	T	β	β+

This table summarizes the data that are displayed in Table S1 with its associated spectra. β, β-strand structure of peptide; β⁺, weak signal; β²⁺, strong signal near 1625 cm⁻¹; C, clear solution; {Dab}, diaminobutyric acid; F, flocculent precipitate; max@, wavelength of maximal ellipticity in the spectra that does not match any typical secondary structure; min@, wavelength of minimal ellipticity in the spectra that does not match any typical secondary structure; NC, no visible change in appearance; O, ornithine; RC, random coil-like structure; T, translucent precipitate; -, signal too weak to interpret; –, no signal.