Parameters influencing scaffold conformation.

A) CD spectra and B) ThT fluorescence of tetrapalmitoylated peptides with shortened length, 9 or 5 amino acids (Palm1–9 in blue and Palm1–5 in orange respectively) or different order of amino acids, reverse or scrambled (Palm15-1 in green and scPalm15 in red, respectively) to model sequence Palm1–15. C) CD and D) ThT of tetrapalmitoylated peptides with different isoelectric point with pI (and net charge) value indicated on top of each column (Palm1–15(D7K) in green, Palm1–15(E3A, D7K) in blue, Palm1–15(E3K, D7K) in orange, Palm1–15(E3K, D7K, E11K) in red and Palm1–15 in black). E) CD and F) ThT of peptides with different number/position of palmitic chains (Palm1–15(1C) in orange, Palm1–15(2C) in red, Palm1–15(1N1C) in green, Palm1–15(4C) in blue and Palm1–15 in black). G) CD and H) ThT of peptides acylated with different lipid chain length (Acetyl1–15 in orange, Butyl1–15 in blue, Octyl1–15 in green, Dodecyl1–15 in red and Palm1–15 in black). Peptides were 30 µM in 2% HFIP/PBS (v/v) (CD) and 15 µM in 1% HFIP/PBS (v/v) (ThT, 24 µM). Fluorescence was measured at 485 nm with excitation at 440 nm. Values are the average of 3 replicates, normalized to the Palm1–15 emission (taken as 100%).