Probing peptide-nanomaterial interactions

Chem Soc Rev. 2010 Sep;39(9):3454-63. doi: 10.1039/b918035b. Epub 2010 Jul 30.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Animals
  • Humans
  • Nanostructures / chemistry*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism*

Substances

  • Peptide Fragments