| Summary: | The work herein investigates the surface active properties of short peptides and their interactions with conventional surfactants. Short peptides can be designed to mimic the structures of conventional surfactants such as SDS and C12TAB. Such peptide structures include V6K peptide, which are attractive in many fields and applications as they can be more biocompatible, biodegradable and environmentally friendlier substitutes to harsh surfactants. Similar peptide structures can also be found naturally occurring in proteins, such as silk fibroin, and can then be liberated by breaking down the protein into its constituent peptides. The interaction of these peptides with conventional surfactants at the air-liquid and solid-liquid interface have not been investigated before. The adsorption behaviour and structures formed at the solid-liquid interface were examined using Ellipsometry and Neutron Reflection.
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