Peptide self-assembly has received considerable attention in the recent years. The reasons are essentially three fold. Peptide fibrillation and amyloid formation appear to be somehow associated with more than 20 neuro-degenerating diseases. Secondly, there are many peptide based materials with potential applications in nano- and medical technology. Furthermore, the number of peptide-based drugs on the market is rapidly growing, and for the formulation at higher concentrations, aggregation can be an issue. Small peptides may self-assemble in solution into well defined b-sheet based structures of various shapes like ribbons, rods, plates or tubes. The aqueous self-assembly is typically driven by hydrophobic interactions but much of peptide self-assembly is far from understood. For example, it is not always clear whether the observed self-assembly corresponds to equilibrium “micelles”, characterized by an equilibrium size distribution, or to kinetically stable precipitates “nanoparticles”. In an attempt to be systematic, we characterized the aqueous self-assembly behavior within the homologous peptide series AnK (alanlys) with n=4, 6, 8 and 10. In this talk we will discuss structural variations and address a number of open questions.

Aqueous self-assembly of AnK peptides

254th National Meeting (2017)

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