Novel fluorescence biosensor custom-made for protein tyrosine phosphatase 1B detection based on titanium...

This paper presents a new fluorescent approach for the detection of protein tyrosine phosphatase 1B (PTP1B) based on titanium dioxide-decorated single-wall carbon nanohorns (TiO₂-SWCNHs). The novel TiO₂-SWCNHs nanocomposite was synthesized and characterized for the first time and the phosphorylated peptide as the substrate of PTP1B was designed. Properties of SWCNHs and TiO₂ were combined by growing nano-sized TiO₂ particles on SWCNHs, resulting in TiO₂-SWCNHs. TiO₂ provides SWCNHs a large adsorption surface area and can specifically bind to phosphopeptide substrate. TiO₂-SWCNHs effectively quenched the fluorescence of the phosphorylated peptide substrate labeled by the fluorophore, and the system had a low fluorescence background. In the presence of PTP1B, dephosphorylation of the peptide occurred owing to the reaction between PTP1B and the peptide, causing the separation of the dye-labeled peptide from TiO₂-SWCNHs, which resulted in fluorescence enhancement of the reaction system. Thus, a simple and rapid strategy for the detection of PTP1B activity was developed, with a detection limit of 0.01 ng/mL and linear range of 0-10 ng/mL. The system can be used to detect PTP1B in serum using the standard addition method. This system provides a new approach for screening PTP1B inhibitors.