Depletion of protein thiols and the accumulation of oxidized thioredoxin in Parkinsonism disclosed by a red-emitting and environment-sensitive probe. Issue 16 (26th March 2019)

• Record Type: Journal Article
• Authors: Hu, Guodong; Zhang, Baoxin; Zhou, Pengcheng; Hou, Yanan; Jia, Huiyi; Liu, Yuxin; Gan, Lu; Zhang, Hong; Mao, Yiheng; Fang, Jianguo
• Is Part Of: Journal of materials chemistry. Volume 7:Issue 16(2019)
• Page Start: 2696
• Page End: 2702
• Publication Date: 2019-03-26
• Subjects: Materials -- Periodicals; Chemistry, Analytic -- Periodicals; Biomedical materials -- Research -- Periodicals; 543.0284
• DOI: 10.1039/c8tb03101k
• Languages: English
• ISSNs: 2050-750X

Abstract

Abstract : Protein sulfhydryl groups play a vital role in maintaining cellular redox homeostasis and protein functions and have attracted increasing interests for the selective detection of protein thiols over low-molecular-weight thiols (LMWTs). Abstract : Protein sulfhydryl groups play a vital role in maintaining cellular redox homeostasis and protein functions and have attracted increasing interests for the selective detection of protein thiols over low-molecular-weight thiols (LMWTs). Herein, we reported a red-emitting and environment-sensitive probe (FM-red ) for detecting and labeling protein thiols. The probe contains a maleimide unit as a thiol receptor and an environment-sensitive fluorophore as a sensor. The emission signal of the probe was exclusively switched on by binding to protein sulfhydryl groups through the twisted intramolecular charge transfer mechanism, while negligible fluorescence was observed whenFM-red reacted with LMWTs. Various experiments verified thatFM-red possessed fast responsivity (∼10 min) and high selectivity to sense protein thiols over LMWTs with a red emission (∼655 nm). These favorable properties enable the probe to image protein sulfhydryl groups in live cells and in vivo . In addition, asFM-red has a relatively high molecular weight (MW 688), it is able to separate the labeled proteins from the unlabeled ones afterFM-red derivatization via routine protein electrophoresis, which may be applied to determine the redox states of thioredoxin, a small redox protein ubiquitous in all cells. With the aid of the probe, we demonstrated a significant decrease in the protein thiols and the accumulation of oxidized thioredoxin in a cellular model of Parkinson's disease.