Protein immobilization in hollow nanostructures and investigation of the adsorbed protein behavior

Xi Qian, Alex Levenstein, Jennifer E. Gagner, Jonathan S. Dordick, Richard W. Siegel

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1295-1303
Number of pages9
JournalLangmuir
Volume30
Issue number5
DOIs
StatePublished - Feb 11 2014

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