Figure 1

CD spectral changes of the peptides upon hemin titration. Spectra were collected at 25 µM peptide upon consecutive addition of molar equivalents (eq) of hemin in PBS. For better visual inspection non-uniform ellipticity scales are applied. The induced secondary structure is helical for most peptides except for buforin that retains significant disorder. The overall intensity is reduced for melittin, CM15, temporin, lasioglossin, and Dhvar4, compared to the higher relative signals for macropin, and FK-16. The helical character of LL-37 is preserved in the presence of hemin.