Confinement effects on the conformation, dynamics and phase transitions of biomolecular systems

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The aim of our project is to explore the effects of geometry, hydroaffinity and softness of confinement conditions on the structure, dynamics and phase behavior of biomolecular and supramolecular systems. We plan to study the effect of geometrical restrictions on the conformation, dynamics and "inverse phase transition" of the model peptide elastin, as well as the selfassociation and aggregation of amyloidogenic peptides, focusing on the initial nucleation and growth process of amyloid fibrils. In addition to concluding measurements on the islet amyloid polypeptide (IAPP), we are planning to study confinement effects on the self-assembly and fibril formation of polylysine stereoisomers. Moreover, we aim at investigating the intermolecular interactions and dynamics of dense protein solutions as well as their phase behavior in the region of the solid-liquid and liquid-liquid phase separation region in well-defined nanoporous structures, including variations of the confinement conditions (i.e., the size, form, heterogeneity of the confinement, and the chemical nature of the walls). Finally, the effects of soft and hard matter confinement on the structure (topology) and phase behavior of lipid mesophases will be studied.