The development of modern peptide chemistry has opened for the possibility of
custom peptide synthesis that allows for systematically investigating the relationship between a specific oligopeptide molecular structure and the macroscopic phases and structures formed in such systems. Understanding the assembly behavior of peptides is important in not only designing nanomaterials for a desired functionality but also for combating neurodegenerative diseases such as Alzheimer and Parkinson’s disease which are strongly associated with an accumulation of amyloid forming peptides in the brain. In this newly started project we focus initially on the self-assembly behavior of short simple and synthetic petides, AnK, where n is varied in the range 4-10 (A=alanine, L=lysine). These peptides allows for a systematic investigation of e.g. the hydrophobicity and peptide length on the self-assembly behavior. A6K in water forms very long hollow nanotubes with a (monodiperse) diameter of 52 nm. Because of the large aspect ratio, the nanotubes form a nematic phase or a hexagonal phase. The nanotube walls are crystalline and the tube formation involves crystal growth processes including oriented fragment attachments. Increasing the peptide concentration, close packing is obtained and there is a first order phase transition to a lamellar phase with the peptide now forming planar bilayers. Increasing the number of hydrophobic alanines to A8K and A10K, aggregation begins at lower peptide concentrations. Also, they do not aggregate into tubes. Instead they form fibrils, a few 100 nm long, with a rectangular cross section of ca. 8 nm x 4 nm.