Probing peptide–nanomaterial interactions

Abstract

Peptide enabled synthesis of nanomaterials offer the ability to control size distributions; morphologies; and provide a range of surface functionalities. Invariably, these qualities are determined by how well peptides are able to interact with nanomaterials via their primary amino acid sequence and/or secondary structure. At present, though, the effect of the primary and secondary peptide structure on peptide–nanomaterial interactions is not well understood and lacks precise characterization with regard to peptide binding interactions. This shortcoming is even further complicated due to the fact that each peptide–nanomaterial interaction is unique for a given set of peptides and nanoparticles. As a result, the behavior of peptides in the presence of nanomaterials requires a separate study and individual consideration on a peptide per peptide basis. Because of this, the effectiveness of peptide–nanoparticle complexes is often “hit or miss” under experimental conditions and when challenged with large sets of potential nanoparticle-binding peptides. In the following tutorial review, we highlight relevant peptide–nanoparticle interactions, describe binding and structural data for these interactions, and provide a general description of appropriate biochemical and physical characterization techniques adopted from materials science, structural biology, and biochemistry to probe synthetically produced peptide–nanoparticle complexes.