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 Forster’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.
Published Version
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