Abstract
A highly sensitive fluorescence method for glycoprotein detection has been established based on fluorescence resonance energy transfer (FRET) between CuInS2 quantum dots (QDs) and rhodamine B (RB). Lectins comprise a group of proteins with unique affinities toward carbohydrate structures, so the process of FRET can occur between lectin-coated QDs (CuInS2 QDs-Con A conjugates, acceptors) and carbohydrate-coated RB (RB-NH2-glu conjugates, donors). The fluorescence of lectin-coated QDs was recovered in the presence of a glycoprotein such as glucose oxidase (GOx) and transferrin (TRF), which significantly reduced the FRET efficiency between the donor and the acceptor. Under optimal conditions, a linear correlation was established between the fluorescence intensity ratio I654/I577 and the TRF concentration over the range of 6.90 × 10(-10) to 3.45 × 10(-8) mol/L, with a detection limit of 2.5 × 10(-10) mol/L. The linear range for GOx is 3.35 × 10(-10) to 6.70 × 10(-8) mol/L, with a detection limit of 1.5 × 10(-10) mol/L. The proposed method was applied to the determination of glycoprotein in human serum and cell-extract samples with satisfactory results. Furthermore, CuInS2 QDs-Con A conjugates are used as safe and efficient optical nanoprobes in HepG2 cell imaging.
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