Conformation and Aggregation of Peptides at Interfaces

Abstract

Conformation of proteins and peptides are not solely determined by their sequence, but are also strongly dependent on the environmental conditions. In addition to factors like salt concentration or pH, the environment presented by the surrounding molecules also play a major role in the conformational preference of proteins and peptides. In this study, we perform a comparative study on the conformational behavior of peptides in bulk vs. at an interface. The interface can be a macroscopic air/water interface or a nanoscale interface presented by the surrounding molecules. I will discuss our research on the interplay of intermolecular forces and influence of interfaces. In the first part the amphiphilic nature of short peptide oligomers and their behavior at the air/water interface will be discussed. The surface driving force and its decomposition will be analyzed. In the second part aggregation of peptides in bulk water and at an interface will be discussed. Different design features which can be tuned to control aggregation behavior will be analyzed. Finally, I will talk about the coarse-grain modeling of peptide-based materials.