Cytochrome c on Silica Nanoparticles: Influence of Nanoparticle Size on Protein Structure, Stability, and Activity

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 loca...

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Bibliographic Details
Published in:Small (Weinheim an der Bergstrasse, Germany) Germany), 2009-02, Vol.5 (4), p.470-476
Main Authors: Shang, Wen, Nuffer, Joseph H., Muñiz-Papandrea, Virginia A., Colón, Wilfredo, Siegel, Richard W., Dordick, Jonathan S.
Format: Article
Language:English
Subjects:
Adsorption
cytochrome c
Cytochromes c - chemistry
Enzyme Stability
Nanoparticles
Particle Size
peroxidase
Protein Conformation
proteins
silica
Silicon Dioxide
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Summary: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 solvent‐accessible 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. Adsorption of cytochrome c (cyt c) onto silica nanoparticle (SNP) surfaces induces changes in protein structures and properties. Cyt c on SNPs with larger sizes experiences greater changes in the global structure and stability. The local heme microenvironment within the protein structure also shows a more pronounced particle‐size dependent disruption on larger SNPs than on smaller ones (see image).
ISSN:1613-6810
1613-6829
DOI:10.1002/smll.200800995