Self-Assembled Peptide Hydrogel as a Smart Biointerface for Enzyme-Based Electrochemical Biosensing and Cell Monitoring

A self-assembled peptide nanofibrous hydrogel composed of N-fluorenylmethoxycarbonyl-diphenylalanine (Fmoc-FF) was used to construct a smart biointerface. This biointerface was then used for enzyme-based electrochemical biosensing and cell monitoring. The Fmoc-FF hydrogel had two functions. One was as a matrix to embed an enzyme model, horseradish peroxidase (HRP), during the self-assembly of Fmoc-FF peptides. The other was use as a robust substrate for cell adhesion. Experimental data demonstrated that HRP was immobilized in a stable manner within the peptide hydrogel, and that HRP retained its inherent bioactivity toward H2O2. The HRP also can realize direct electron transfer in the Fmoc-FF hydrogel. The resulting third-generation electrochemical H2O2 biosensor exhibited good analytical performance, including a low limit of detection of 18 nM, satisfactory reproducibility, and high stability and selectivity. HeLa cells were then adhered to the HRP/Fmoc-FF hydrogel-modified electrode. The sensitive in situ monitoring of H2O2 released from HeLa cells was realized. This biointerface based on the Fmoc-FF hydrogel was easily prepared, environmentally friendly, and also versatile for integration of other cells and recognized molecules for the monitoring of various cellular biomolecules. The smart biointerface has potential application in broad physiological and pathological investigations.