Amyloid-like protein nanofibrous membranes as a sensing layer infrastructure for the design of mass-sensitive biosensors

AL-BSA modified surfaces were characterized by X-ray photoelectron spectroscopy (XPS), scanning electron microscope (SEM), quartz crystal microbalance (QCM), contact angle (CA) and attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR). Protein detection was measured based on the frequency shift before and after the covalent bonding of Lys. Under optimized conditions, the proposed immobilization platforms could bind 335 ng/mL and 250 ng/mL of Lys for batch and continuous processes, respectively. Our results demonstrate the potential usage of these self-functional electrospun AL-BSA infrastructure sensing layers on QCM surfaces. This modification enables the direct immobilization of bioactive agents by eliminating any surface functionalization process for further mass-sensitive biosensor applications.