Studies on the interactions of 3,6-diaminoacridine derivatives with human serum albumin by fluorescence spectroscopy
LUMINESCENCE, cilt.29, sa.7, ss.872-877, 2014 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 29 Sayı: 7
- Basım Tarihi: 2014
- Doi Numarası: 10.1002/bio.2635
- Dergi Adı: LUMINESCENCE
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.872-877
- Anahtar Kelimeler: human serum albumin, acridine, proflavine, Stern-Volmer, FRET, RESONANCE ENERGY-TRANSFER, ACRIDINE-DERIVATIVES, QUENCHING METHOD, BINDING, PROFLAVINE, ACYLATION, AGENTS, DRUGS, BSA, DNA
- Gazi Üniversitesi Adresli: Evet
Özet
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.