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Optical interrogation of oligomeric proteins in human brain tissues from Parkinson’s disease

Quantifying the protein expression level and detecting aberrant proteins are critical to many therapeutic areas such as cancer development, brain injury, inflammation and infectious diseases. However, it is difficult to detect a small trace of the proteins, and it is challenging and even controversial to reveal their oligomerization state, which is often a hallmark of numerous neurodegenerative diseases. To understand pathophysiological mechanisms of Alzheimer’s disease and Parkinson’s disease, it is urgent to establish a robust, quantitative and highly sensitive method that precisely diagnoses accumulation of the oligomer and aggregate of proteins.

Benjamin Croop and Jialei Tang, graduate students of Optical Nanoscopy Lab led by Dr. Kyu Young Han applied single-molecule pull-down (SiMPull) technique to directly count the number of proteins and reveal the stoichiometry of the oligomer proteins. They used (i) single-molecule total internal reflection fluorescence microscopy to visualize proteins captured by fluorescently labeled antibody, and (ii) in vivo crosslinker to preserve native states of biological samples including cultured cells and postmortem brain tissues. This powerful single-molecule assay can be highly useful in diagnostic applications using various specimens for neurodegenerative diseases including Alzheimer’s disease and Parkinson’s disease. This work was accomplished by the collaboration with Dr. Yoon-Seong Kim’s lab at Burnett School of Biomedical Sciences, and has been published in this week Analytical Chemistry.

Posted Wednesday, November 29, 2017

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