A near-infrared fluorescent probe quinaldine red lights up the β-sheet structure of amyloid proteins in mouse brain.

In this report, we describe a near-infrared fluorescent probe called quinaldine red (QR) which lights up the β-sheet structure of amyloid fibrils. The photochemical and biophysical properties of QR along with other canonical amyloid probes in the presence of protein fibrils were investigated by using fluorescence spectroscopy, confocal fluorescent microscopy and isothermal titration calorimetry. Moreover, the binding sites and interaction mode between QR and insulin fibrils were calculated based on molecule docking. Among these amyloid probes, QR showed several advantages including strong supramolecular force, near-infrared emission, high sensitivity and resistance to bleaching. A linear response of the fluorescence intensity of QR towards fibril samples in the presence of sera was visualized in the range of 1-30 μM, with the limit of detection (LOD) of 2.31 μM. The recovery and relative standard deviation (RSD) of the proposed method for the determination of protein fibrils was 90.4%-99.2% and 3.05%-3.47%, respectively. Finally, QR can be fluorescently lighted up when meeting the aberrant protein aggregates of pathogenic mice. We recommend QR as a novel and excellent alternative tool for monitoring conformational transition of amyloid proteins.