MLMengyao Li

Mengyao Li

*This is an algorithmically generated author record based on publicly available information.

Mengyao Li has a total of 5 co-authors. Here are the top co-authors by number of shared publications:

  • Chen Zhai

    COFCO Nutrition and Health Research Institute, Beijing Key Laboratory of Nutrition and Health and Food Safety, Beijing 102209, PR China

    1 shared publication
  • Shuya Wang

    Nutrition & Health Research Institute, COFCO Corporation, Beijing Key Laboratory of Nutrition & Health and Food Safety, Beijing 102209, China

    1 shared publication
  • Weixia Huang

    Nutrition & Health Research Institute, COFCO Corporation, Beijing Key Laboratory of Nutrition & Health and Food Safety, Beijing 102209, China

    1 shared publication
  • Yunguo Liu

    College of Life Science and Technology, Xinjiang University, Urumqi 830002, China

    1 shared publication
  • Zhao Li

    Shaanxi Engineering Laboratory for Food Green Processing and Safety Control, and Shaanxi Key Laboratory for Hazard Factors Assessment in Processing and Storage of Agricultural Products, College of Food Engineering and Nutritional Science, Shaanxi Normal University, Xi’an 710062, China

    1 shared publication

Latest Publications

  • Open Access

    Detection of carboxylesterase by a novel hydrosoluble near-infrared fluorescence probe

    by Mengyao Li, Chen Zhai, Shuya Wang, Weixia Huang, Yunguo Liu, Zhao Li

    A novel hydrosoluble near-infrared fluorescence off–on probe has been developed for detecting carboxylesterase activity. The probe was designed by introducing (4-acetoxybenzyl)oxy as a quenching and recognizing moiety to the decomposed product of IR-783, which exhibits excellent near-infrared fluorescence features and good water solubility. The responding mechanism of novel probe 1 to carboxylesterase was investigated. It would lead to the cleavage of the carboxylic ester bond by carboxylesterase catalyze the spontaneous hydrolysis of the probe, resulting in the release of a near-infrared fluorophore. This behaviour leads to the development of a simple and sensitive fluorescent method for assaying carboxylesterase activity, with a detection limit of 3.4 × 10−3 U mL−1. Moreover, the probe displays excellent selectivity toward carboxylesterase over other substances. Notably, the imaging experimental results showed that the probe 1 is cell membrane permeable, and its applicability has been demonstrated for monitoring carboxylesterase activity in HeLa cells.