Rational design and self-assembly of short amphiphilic peptides and applications

Abstract

Peptide self-assembly is an effective way to construct well-ordered nanostructures for biomedical applications. Given that short peptide length always facilitates large-scale production for future applications and the easy establishment of structure-property relationship, this review highlights recent advances in the self-assembly of short amphiphilic peptides, focusing on the strategies to manipulate the involved non-covalent interactions as well as the consequent supramolecular architectures. One representative strategy is based on molecular design, in which amino acid substitution, sequence variation, terminal capping, molecular geometry, and amino acid chirality are considered. Another important strategy that varies solution conditions (pH, solvents, enzymes, and metal ions) is also discussed. A variety of self-assembled pep1tide nanostructures and nanomaterials have been achieved therefrom and more importantly, the advances make the prediction of peptide self-assembly increasingly feasible based on a certain class of peptide sequences and solution conditions. Additionally, their applications as antibiotics and templates for nanofabrication, mainly from the work of our group, demonstrate the importance of the surface properties and morphologies of self-assemblies to practical applications. Following previous studies, future endeavor in this field is suggested to focus on designing more peptide sequences with functional motifs not only to summarize general rules to predict self-assembly but also to realize practical applications.