American Chemical Society
ja0632411_si_001.pdf (32.59 kB)

Aggregation of the Amphipathic Peptides (AAKA)n into Antiparallel β-Sheets

Download (32.59 kB)
journal contribution
posted on 2006-10-18, 00:00 authored by Thomas J. Measey, Reinhard Schweitzer-Stenner
Helical wheel projections of peptides based on the repeating unit Ac-(AAKA)n-NH2 clearly illustrate an amphipathic nature. One should therefore expect these peptides to form helices if the number of residues exceeds a certain threshold value. Indeed, ECD measurements show that Ac-(AAKA)4-NH2 and, to a minor extent, also Ac-(AAKA)3-NH2 exhibit some helical content at millimolar concentrations in aqueous solution. Surprisingly, however, these peptides were found to form hydrogels with an antiparallel β-sheet conformation at centimolar concentrations. This occurs despite the positively charged lysine side chain which would be expected to inhibit the formation of extended β-sheet layers.