Optimizing the selective recognition of protein isoforms through tuning of nanoparticle hydrophobicity

Nanoscale. 2014 Jun 21;6(12):6492-6495. doi: 10.1039/c4nr01085j.

Abstract

We demonstrate that ligand hydrophobicity can be used to increase affinity and selectivity of binding between monolayer-protected cationic gold nanoparticles and β-lactoglobulin protein isoforms containing two amino acid mutations.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Gold / chemistry*
  • Hydrophobic and Hydrophilic Interactions
  • Lactoglobulins / chemistry*
  • Lactoglobulins / genetics
  • Lactoglobulins / ultrastructure*
  • Materials Testing
  • Metal Nanoparticles / chemistry*
  • Metal Nanoparticles / ultrastructure
  • Mutagenesis, Site-Directed
  • Nanocomposites / chemistry*
  • Nanocomposites / ultrastructure
  • Particle Size
  • Protein Binding
  • Protein Isoforms / chemistry
  • Protein Isoforms / ultrastructure
  • Structure-Activity Relationship

Substances

  • Lactoglobulins
  • Protein Isoforms
  • Gold