Terminal protection of peptides by interactions with proteins: A "signal-on" peptide-templated gold nanocluster beacon for label-free protein detection.

Characterization of the protein-peptide interactions are a critical for understanding the functions and signal pathways of proteins. Herein, a new finding of universal terminal protection that protein bind specifically with peptide and provide a protective coating to prevent peptide hydrolysis in the presence of peptidase. On the basis of this mechanism, we first reported a novel label-free fluorescence biosensor strategy that utilizes the protection of specific terminal protein on peptide-templated gold nanocluster (AuNCs) beacon for the detection of proteins. The fluorescence quenching of peptide-templated AuNCs can be effectively inhibited with increasing concentration of the specific protein, exhibiting a satisfactory sensitivity and selectivity toward protein with the detection limit of MDM2 and gp120 are 0.0019 U/mL and 0.0012 U/mL, respectively. The developed label-free fluorescence biosensor strategy provides new ideas to detect and screen protein for analyzing protein-peptide interaction in biomedical applications.