Abstract
We synthesized a new probe, 4-[2-(2-naphthyl)-(E)-ethenyl]-benzyl(triphenyl)phosphonium bromide (NEB), to detect the formation of amyloid fibrils of bovine insulin. The fluorescence intensity of NEB in the presence of insulin fibrils was 30 times higher than that before fibrillation, with the fluorescence quantum yield increased from 2.5% to 78%. In comparison with the commercially available probe, thioflavin T (ThT), NEB exhibits a 10 times stronger fluorescence and a shorter identification lag phase for detecting insulin fibrillation, indicating a higher sensitivity in detection of insulin oligomers and fibrils.
Highlights
Amyloid brils are a denatured brous form of protein aggregates, and have been extensively investigated because their deposition causes several serious diseases, such as Alzheimer's and Parkinson's diseases, type II diabetes and prion diseases.[1]
To verifying that NEB belongs to a class of molecular rotors,[15] we dissolved NEB in a mixture of ethanol and glycerol
The concentration of glycerol was varied from 0% to 80% to increase the viscosity
Summary
Amyloid brils are a denatured brous form of protein aggregates, and have been extensively investigated because their deposition causes several serious diseases, such as Alzheimer's and Parkinson's diseases, type II diabetes and prion diseases.[1]. Compared to ThT, NEB exhibits a 10 times stronger uorescence intensity upon binding to the insulin brils which arise from the increased the kr and decreased knr.
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