Abstract
The interactions between hemoglobin (Hb) and itraconazole (ITZ) are investigated in details using UV–vis spectra, circular dichroism spectroscopy, steady state fluorescence, three-dimensional fluorescence spectra, synchronous fluorescence and time-resolved fluorescence spectra at molecular level. The UV–vis studies represent that ITZ can access into heme group and lead to it explored in aqueous medium. CD spectra suggest ITZ could combine with amino acid residues in polypeptide chain and cause a partial unfolding of Hb (reducing of the α-helix content). Steady state fluorescence/synchronous fluorescence (taking into account inner filter effects) and three-dimensional fluorescence/time-resolved fluorescence spectroscopy results reveal that ITZ alters polarity and conformation around the fluorophore molecule. The interaction processes are static quenching mechanisms. The negative of ΔH0 and ΔS0 indicate that hydrogen bonds and van der Waals are the main force.
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