ABSTRACT
Exploiting cellulose nanocrystals' high aspect ratio and tailorable surface for immunological biosensors has been hindered by the relatively limited research on using commonly available sulfated cellulose nanocrystals (CNCs) for antibody immobilization and by the low hydrolytic stability of dried assemblies produced from sulfated CNCs. Herein, we report a reaction scheme that enables both hydrolytic stability and antibody immobilization through 3-aminopropyl-triethoxysilane and glutaric anhydride chemistry. Immobilization was demonstrated using three model antibodies used in the detection of the cancer biomarkers: alpha-fetoprotein, prostate-specific antigen, and carcinoembryonic antigen. Thermogravimetric analysis coupled with Fourier-transform infrared spectroscopy provided evidence of CNC modification. Quartz crystal microbalance with dissipation monitoring was used to monitor binding during each step of the immobilization scheme as well as binding of the corresponding antigens. The general reaction scheme was tested using both aqueous CNC dispersions and CNC films. Film modification is slightly simpler as it avoids centrifugation and washing steps. However, modifying the dispersed CNCs provides access to their entire surface area and results in a greater capacity for antigen binding.
