Cytochrome c on silica nanoparticles: Influence of nanoparticle size on protein structure, stability, and activity

Wen Shang, Joseph H. Nuffer, Virginia A. Muñiz-Papandrea, Wilfredo Colón, Richard W. Siegel, Jonathan S. Dordick

Research output: Contribution to journalArticlepeer-review

205 Scopus citations

Abstract

The structure, thermodynamic and kinetic stability, and activity of cytochrome c (cyt c) on silica nanoparticles (SNPs) of different sizes have been studied. Adsorption of cyt c onto larger SNPs results in both greater disruption of the cyt c global structure and more significant changes of the local heme microenvironment than upon adsorption onto smaller SNPs. The disruption of the heme microenvironment leads to a more solventaccessible protein active site, as suggested by Soret circular dichroism spectroscopy and through an increase in peroxidase activity as a function of increased SNP size. Similarly, the stability of cyt c decreases more dramatically upon adsorption onto larger SNPs. These results are consistent with changes in protein-nanoparticle interactions that depend on the size or surface curvature of the supporting nanostructure. This study provides further fundamental insights into the effects of nanoscale surfaces on adsorbed protein structure and function.

Original languageEnglish
Pages (from-to)470-476
Number of pages7
JournalSmall
Volume5
Issue number4
DOIs
StatePublished - 20 Feb 2009
Externally publishedYes

Keywords

  • Cytochrome c
  • Nanoparticles
  • Peroxidase
  • Proteins
  • Silica

Fingerprint

Dive into the research topics of 'Cytochrome c on silica nanoparticles: Influence of nanoparticle size on protein structure, stability, and activity'. Together they form a unique fingerprint.

Cite this