Studies on the interactions of 3,6-diaminoacridine derivatives with human serum albumin by fluorescence spectroscopy

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GÖKOĞLU E., KIPCAK F., Seferoglu Z.

LUMINESCENCE, vol.29, no.7, pp.872-877, 2014 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 29 Issue: 7
  • Publication Date: 2014
  • Doi Number: 10.1002/bio.2635
  • Journal Name: LUMINESCENCE
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.872-877
  • Hacettepe University Affiliated: Yes


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 Delta H, Delta S and Delta G were calculated at different temperatures. The binding distance (r) similar to 3 nm between the donor (HSA) and acceptors (3,6-diethoxycarbonyl aminoacridine, 3,6-diphenoxycarbonyl aminoacridine and proflavine) was obtained according to Forster's non-radiative energy transfer theory. Moreover, the limit of detection and limit of quantification of derivatives were calculated in the presence of albumin. Copyright (C) 2014 John Wiley & Sons, Ltd.