Spatiotemporal control of the creation and immolation of peptide assemblies

• Peptide assemblies can chemically and structurally emulate the functions of naturally occurring nanostructures.
• The selective disassembly and breakdown of peptide assemblies is equally important for their use as biomaterials.
• Spatiotemporal control has become an increasingly important guiding principle for the development of peptidic biomaterials.

Peptides are excellent building units to construct supramolecular biomaterials for diverse biomedical applications. A vast amount of research effort over the past two decades has focused on the rational design of peptidic building units and the formulation protocols required to create supramolecular assemblies that can chemically and structurally emulate the functions of naturally occurring nanostructures. A rapidly growing interest in the field is the spatiotemporal regulation of the formation and immolation pathways of peptide assemblies, an essential characteristic to control if these constructs are to fulfill their roles as biologically active and compatible materials. In this review, we discuss the necessity for control over the assembly and morphological transformation of peptides and peptide conjugates, the critical role of these properties for their ultimate biological application, as well as the methods by which this can be programmed into the molecular structure. A particular focus will be on recent advances in the use of enzyme and redox processes for exerting spatiotemporal control over a variety of peptide-based nanostructures.