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Characterization of Phenosafranine–Hemoglobin Interactions in Aqueous Solution

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Abstract

Binding of the drug phenosafranine to hemoglobin (Hb) in aqueous solutions was investigated by fluorescence, UV/vis and circular dichroism (CD) spectral methods at pH=7.4. The fluorescence data showed that fluorescence quenching of Hb by phenosafranine is the result of formation of a phenosafranine–Hb complex with a 1:1 molar ratio. Thermodynamic analysis implied that hydrophobic, electrostatic and hydrogen bond interactions are all involved in stabilizing the complex. The molecular distance (r=4.29 nm) between the donor (Hb) and acceptor (phenosafranine) was calculated according to Förster’s theory. The features of phenosafranine-induced secondary structure changes of Hb have been studied by synchronous fluorescence, CD and three-dimensional fluorescence spectroscopy. This study improves our knowledge of the interaction dynamics of phenazinium drugs to the physiologically important protein Hb.

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Abbreviations

Hb:

hemoglobin

Trp:

tryptophan

Tyr:

tyrosine

Phe:

phenylalanine

CD:

circular dichroism

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Authors and Affiliations

  1. College of Economics and Management, China Agricultural University, Beijing, 100083, China

    Wei Liu

  2. Department of Chemistry, China Agricultural University, Beijing, 100193, China

    Wei Liu, Fei Ding & Ying Sun

Authors
  1. Wei Liu
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  2. Fei Ding
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  3. Ying Sun
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Correspondence to Ying Sun.

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Liu, W., Ding, F. & Sun, Y. Characterization of Phenosafranine–Hemoglobin Interactions in Aqueous Solution. J Solution Chem 40, 231–246 (2011). https://doi.org/10.1007/s10953-010-9647-1

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  • DOI: https://doi.org/10.1007/s10953-010-9647-1

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