Derivatizing Nile Red fluorophores to quantify the heterogeneous polarity upon protein aggregation in the cell

  • Chem Commun (Camb). 2022 Apr 28;58(35):5407-5410. doi: 10.1039/d2cc00629d.
Rui Sun  1  2 ,  Wang Wan  1 ,  Wenhan Jin  1 ,  Yulong Bai  1  2 ,  Qiuxuan Xia  1  2 ,  Mengdie Wang  1  2 ,  Yanan Huang  1 ,  Lianggang Zeng  1 ,  Jialu Sun  1 ,  Congcong Peng  1  3 ,  Biao Jing  1  3 ,  Yu Liu  1
Affiliations
  • 1. CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian 116023, China. [email protected].
  • 2. University of the Chinese Academy of Sciences, Beijing 100049, China.
  • 3. The Second Hospital of Dalian Medical University, 467 Zhongshan Road, Dalian, 116023, China.
PMID: 35415726 DOI: 10.1039/d2cc00629d
Abstract

Protein aggregation in the cell is often manifested by the formation of subcellular punctate structures. Herein, we modulated the solvatochromism and solubility of Nile Red fluorophore derivatives to quantitatively study the polarity inside pathogenic protein aggregates, revealing structure- and protein-dependent polarity heterogeneity.

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