Functional Peptide Monolayers at Interfaces

Amphiphilic peptides can be designed to form ordered supramolecular structures at hydrophilic-hydrophobic interfaces. These systems rely on the ability of peptides to fold into certain secondary structures at interfaces. This review focuses on the design of amphiphilic β-sheet peptide assemblies in monolayers at interfaces, and their relevance to inducing mineralization and interactions with specific ions. In addition, the review discusses recent studies demonstrating the applicability of designed amphiphilic β-sheet peptides to detection of specific small molecules and to elucidating intermolecular interactions relevant to drug delivery and enzyme catalysis systems.