LAUSR

Peptide sequences are known to recognize and bind different nanomaterial surfaces, which has resulted in the screening and identification of hundreds of peptides with the ability to bind to a wide range of metallic, metal oxide, mineral, and polymer substrates. These biomolecules are able to bind to materials with relatively high affinity, resulting in the generation of a complex biointerface between the biotic and abiotic components. While the number of material-binding sequences is large, at present, quantitative materials-binding characterization of these peptides has been accomplished only for a relatively small number of sequences. Moreover, it is currently very challenging to determine the molecular-level structure(s) of these peptides in the materials adsorbed state. Despite this lack of data related to the structure and function of this remarkable biointerface, several of these peptide sequences have found extensive use in creating functional nanostructured materials for assembly, catalysis, energy, and medicine, all of which are dependent on the structure of the individual peptides and collective biointerface at the material surface. In this Review, we provide a comprehensive overview of these applications and illustrate how the versatility of this peptide-mediated approach for the growth, organization, and activation of nanomaterials could be more widely expanded via the elucidation of biointerfacial structure/property relationships. Future directions and grand challenges to realize these goals are highlighted for both experimental characterization and molecular-simulation strategies.