Unfolding of ribonuclease A on silica nanoparticle surfaces.
This paper reports on the unfolding behavior of ribonuclease A (RNase A) on silica nanoparticle surfaces and quantitively demonstrates that nanoscale size and surface curvature play key roles in influencing the stability of adsorbed proteins. Urea denaturation analyses showed that the thermodynamic stability of RNase A decreased upon adsorption onto the nanoparticles, with greater decrease on larger nanoparticles. The stability changes of RNase A correlate well with the changes in the protein-nanoparticle interactions, which increase as the surface contact area and surface charge interaction increases. This study, therefore, provides fundamental information on the effect of nanoscale surfaces on protein structure and function.
Shang
Wen
W
Rensselaer Nanotechnology Center, Department of Materials Science and Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
Nuffer
Joseph H
JH
Dordick
Jonathan S
JS
Siegel
Richard W
RW
D000327:Adsorption; D000818:Animals; D002417:Cattle; D004795:Enzyme Stability; D053758:Nanoparticles; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry* / Q000493:pharmacokinetics; D012822:Silicon Dioxide
D012822:Silicon Dioxide; D012259:Ribonuclease, Pancreatic