title: Engineering the interface between glucose oxidase and nanoparticles.
abstract: The behavior of glucose oxidase (GOx) on gold nanoparticles (NPs) was investigated as a function of (1) NP surface chemistry, (2) stabilizing protein additives, and (3) protein microenvironment. GOx secondary structure and unfolding was probed by circular dichroism (CD) spectroscopy and fluorescence, and GOx enzymatic activity was measured by a colorimetric assay. We also examined the activity and structure of GOx after displacement from the NP surface. Generally, GOx behavior was negatively impacted by conjugation to the NP, and conjugation conditions could vary the influence of the NP. Surface chemistry and protein microenvironment could improve behavior, but addition of stabilizing proteins negatively influenced activity. After displacement from the NPs, GOx tended to remain unfolded, indicating that the interactions with the NP were irreversible.
authors.affiliation: Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States.
authors.forename: Edurne
authors.initials: E
authors.lastname: Tellechea
authors.forename: Kenneth J
authors.initials: KJ
authors.lastname: Wilson
authors.forename: Ernesto
authors.initials: E
authors.lastname: Bravo
authors.forename: Kimberly
authors.initials: K
authors.lastname: Hamad-Schifferli
mesh_terms: D002942:Circular Dichroism; D005949:Glucose Oxidase / Q000737:chemistry / Q000378:metabolism*; D053758:Nanoparticles; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence
chemical_list: D005949:Glucose Oxidase