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Wang Q, Fan J, Zhou Y, et al. Development of a human serum albumin structure-based fluorescent probe for bioimaging in living cells. Spectrochim Acta A Mol Biomol Spectrosc. 2021;269:120769doi: 10.1016/j.saa.2021.120769.
Wang, Q., Fan, J., Zhou, Y., & Xu, S. (2021). Development of a human serum albumin structure-based fluorescent probe for bioimaging in living cells. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 269120769. https://doi.org/10.1016/j.saa.2021.120769
Wang, Qing, et al. "Development of a human serum albumin structure-based fluorescent probe for bioimaging in living cells." Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy vol. 269 (2021): 120769. doi: https://doi.org/10.1016/j.saa.2021.120769
Wang Q, Fan J, Zhou Y, Xu S. Development of a human serum albumin structure-based fluorescent probe for bioimaging in living cells. Spectrochim Acta A Mol Biomol Spectrosc. 2021 Dec 16;269:120769. doi: 10.1016/j.saa.2021.120769. Epub 2021 Dec 16. PMID: 34942415.
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Spectrochim Acta A Mol Biomol Spectrosc. 2021 Dec 16;269:120769. doi: 10.1016/j.saa.2021.120769. Epub 2021 Dec 16.

Development of a human serum albumin structure-based fluorescent probe for bioimaging in living cells.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy

Qing Wang, Jingwen Fan, Youjun Zhou, Shaohu Xu

Affiliations

  1. School of Chemistry and Chemical Engineering, Yangzhou University, Yangzhou 225002, China. Electronic address: [email protected].
  2. School of Chemistry and Chemical Engineering, Yangzhou University, Yangzhou 225002, China.

PMID: 34942415 DOI: 10.1016/j.saa.2021.120769

Abstract

Forming a stable complex is a prerequisite for intramolecular charge transfer (ICT) probe to recognize proteins. Herein, a human serum albumin (HSA) structure-based fluorescent probe DNPM was fabricated successfully with fully considering its binding to the primary sites in HSA. Molecular simulation was used to assist the probe design. Two ICT ligands DNPM and MPM were initially designed. Both DNPM and MPM had favorable HSA binding abilities, but only DNPM had a satisfactory HSA sensitivity. Electromagnetic coupling played a key role in DNPM fluorescence enhancement. Due to the electromagnetic environment difference in protein structure, DNPM only exhibited strong sensitivity to serum albumins. DNPM could bind to Sudlow site I and site II in HSA but could not be displaced from its binding sites by common site specific drugs (e.g. phenylbutazone and ibuprofen). Besides, DNPM exhibited great potential for illumining serum albumin in living cells. The results provided a beneficial approach for designing and synthesizing high sensitive and selective fluorescent probes for proteins.

Copyright © 2021 Elsevier B.V. All rights reserved.

Keywords: Cell imaging; Competitive displacement; Fluorescent probe; Ligand-protein interaction; Molecular simulation

Conflict of interest statement

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this pa

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