title: Studies on the interactions of 3,6-diaminoacridine derivatives with human serum albumin by fluorescence spectroscopy.
abstract: This study reports the preparation and investigation of the modes of binding of the two symmetric 3,6-diaminoacridine derivatives obtained from proflavine, which are 3,6-diphenoxycarbonyl aminoacridine and 3,6-diethoxycarbonyl aminoacridine to human serum albumin (HSA). The interaction of HSA with the derivatives was investigated using fluorescence quenching and ultraviolet-visible absorption spectra at pH 7.2 and different temperatures. The results suggest that the derivatives used can interact strongly with HSA and are the formation of HSA-derivative complexes and hydrophobic interactions as the predominant intermolecular forces in stabilizing for each complex. The Stern-Volmer quenching constants, binding constants, binding sites and corresponding thermodynamic parameters ΔH, ΔS and ΔG were calculated at different temperatures. The binding distance (r) ~ 3 nm between the donor (HSA) and acceptors (3,6-diethoxycarbonyl aminoacridine, 3,6-diphenoxycarbonyl aminoacridine and proflavine) was obtained according to Förster's non-radiative energy transfer theory. Moreover, the limit of detection and limit of quantification of derivatives were calculated in the presence of albumin.
authors.affiliation: Department of Chemistry, Hacettepe University, Ankara, Turkey.
authors.forename: Elmas
authors.initials: E
authors.lastname: Gökoğlu
authors.forename: Fulya
authors.initials: F
authors.lastname: Kıpçak
authors.forename: Zeynel
authors.initials: Z
authors.lastname: Seferoğlu
mesh_terms: D006801:Humans; D015394:Molecular Structure; D011370:Proflavine / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
chemical_list: D012709:Serum Albumin; D011370:Proflavine
keywords: FRET; Stern-Volmer; acridine; human serum albumin; proflavine