Protein immobilization in hollow nanostructures and investigation of the adsorbed protein behavior.
Understanding nanomaterial-biomolecule interactions is critical to develop broad applications in sensors, devices, and therapeutics. During the past decade, in-depth studies have been performed on the effect of nanoscale surface topography on adsorbed protein structure and function. However, a fundamental understanding of nanobio interactions at concave surfaces is limited; the greatest challenge is to create a nanostructure that allows such interactions to occur and to be characterized. We have synthesized hollow nanocages (AuNG) through careful control of morphology and surface chemistry. Lysozyme was used as a model to probe interactions between a protein and these nanostructures. Solid Au nanoparticles with a similar morphology and surface chemistry were also used as a reference. Through a series of quantitative analyses of protein adsorption profiles and enzymatic activity assays of both nanobioconjugates, we discovered that a significant amount of protein could be delivered into the core of AuNG, while maintaining a substantial fraction of native activity.
Department of Materials Science and Engineering, ‡Rensselaer Nanotechnology Center, §Center for Biotechnology and Interdisciplinary Studies, and ∥Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute , Troy, New York 12180, United States.
Xi
X
Qian
Alex
A
Levenstein
Jennifer E
JE
Gagner
Jonathan S
JS
Dordick
Richard W
RW
Siegel
D000327:Adsorption; D006046:Gold / Q000737:chemistry; D055767:Immobilized Proteins / Q000737:chemistry*; D008855:Microscopy, Electron, Scanning; D009113:Muramidase / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties
D055767:Immobilized Proteins; D011506:Proteins; D006046:Gold; D009113:Muramidase