caa a22 4500 445328835 CHVBK 20180317142730.0 cr unu---uuuuu 170323e20111101xx s 000 0 eng 10.1007/s10953-011-9766-3 doi (NATIONALLICENCE)springer-10.1007/s10953-011-9766-3 Multi-spectroscopic Investigations of Aspirin and Colchicine Interactions with Human Hemoglobin: Binary and Ternary Systems [Elektronische Daten] [Hamideh Sanei, Ahmad Asoodeh, Shirin Hamedakbari-Tusi, Jamshidkhan Chamani] The interactions of colchicine (COL) and aspirin (ASA) with human hemoglobin (HB) was studied by fluorescence, UV/vis absorption, resonance light scattering, synchronous fluorescence and circular dichroism (CD) spectroscopic techniques under physiological conditions. The inherent binding information, including the quenching mechanism, binding constants, number of binding sites, effective quenching constant, fraction of the initial fluorescence and thermodynamic parameters were determined by the fluorescence quenching technique at different temperatures. The results proved that the mechanism of fluorescence quenching of HB by COL and ASA is due to formation of HB-drug complexes in the binary and ternary systems. The distance between the acceptor drugs and HB was estimated by Förster's equation on the basis of fluorescence energy transfer. In addition, according to the synchronous fluorescence spectra of HB, the results showed that the fluorescence quenching of HB originated solely from the tryptophan residues and indicated a conformational change for HB caused by addition of the drugs. Far-UV CD spectra of HB were recorded before and after the addition of ASA and COL both as binary and ternary systems. An increase in intensity of the positive CD peak of HB was observed in the presence of these drugs. The results were interpreted as excited state interactions between the aromatic residues of the HB binding sites and the drugs bound to them. Springer Science+Business Media, LLC, 2011 Human hemoglobin nationallicence Aspirin nationallicence Colchicine nationallicence Quenching nationallicence RLS nationallicence Circular dichroism nationallicence Sanei Hamideh Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran aut Asoodeh Ahmad Department of Chemistry, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran aut Hamedakbari-Tusi Shirin Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran aut Chamani Jamshidkhan Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran aut Journal of Solution Chemistry Springer US; http://www.springer-ny.com 40/11(2011-11-01), 1905-1931 0095-9782 40:11<1905 2011 40 10953 https://doi.org/10.1007/s10953-011-9766-3 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10953-011-9766-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Sanei Hamideh Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran aut NATIONALLICENCE 700 1- Asoodeh Ahmad Department of Chemistry, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran aut NATIONALLICENCE 700 1- Hamedakbari-Tusi Shirin Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran aut NATIONALLICENCE 700 1- Chamani Jamshidkhan Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran aut NATIONALLICENCE 773 0- Journal of Solution Chemistry Springer US; http://www.springer-ny.com 40/11(2011-11-01), 1905-1931 0095-9782 40:11<1905 2011 40 10953 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer