Design of amphiphilic peptide nanofibers

Abstract Peptide molecules self-assemble into a variety of supramolecular nanostructures. The interactions among the peptide molecules can be controlled by intrinsic properties of the amino acid side chains and by conjugation of molecules to the reactive sites. Noncovalent interactions among the peptide molecules provide opportunities for fabrication of aggregates through self-assembly method. The peptide self-assembly is affected by external stimuli similar to secondary structures in proteins. The peptide self-assembly can be programmed by stimuli-responsive molecules and the programmable molecules are used for fabrication of bioinspired functional materials. In addition to natural amino acids, various synthetic amino acids are also used to create a diverse set of self-assembling building blocks. Orthogonal protecting group chemistry and solid-phase peptide synthesis methods provide vast opportunities for synthesis of diverse peptides and enable development of supramolecular functional materials. In this chapter, design principles, applications, and characterizations of the amphiphilic peptides will be discussed.