Probing peptide-nanomaterial interactions.
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.
Slocik
Joseph M
JM
Nanostructured and Biological Materials Branch, Materials and Manufacturing Directorate, Air Force Research Lab, Wright-Patterson AFB, OH 45433, USA.
Naik
Rajesh R
RR
D000818:Animals; D006801:Humans; D049329:Nanostructures / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*
D010446:Peptide Fragments