caa a22 4500 605507112 CHVBK 20210128100630.0 cr unu---uuuuu 210128e20150901xx s 000 0 eng 10.1007/s00775-015-1287-x doi (NATIONALLICENCE)springer-10.1007/s00775-015-1287-x Exploring the copper(II)-aminotriazole complex-binding sites of human serum albumin [Elektronische Daten] [Lijun Yang, Lian He, Jing Zhang, Shuai An, Lei Zhang] The potential impact on human exposure to aminotriazole (ATA) and heavy metal in the environment becomes a concerning issue. In the current study, a water-soluble Cu(II)-aminotriazole complex [Cu(II)-ATA] was synthesized. To explore the binding mechanism of the complex with human serum albumin (HSA), their effects on conformation and activity of HSA by multispectroscopic approach and molecular modeling were investigated. Further fluorescent tests revealed that the quenching mechanism of HSA by Cu(II)-ATA was overall static. Meanwhile, the obtained binding constant and thermodynamic parameters on complex-HSA interaction showed that the types of interaction force of Cu(II)-ATA and HSA were hydrogen bonding, van der Waals and electrostatic. The analysis of three-dimensional fluorescence, circular dichroism and Fourier transform infrared spectroscopy showed that Cu(II)-ATA induced the changes in the secondary structure of HSA. Molecular docking simulation was performed and docking model suggested that the complex docked into HSA at subdomain IIA. Furthermore, amino group and attractive electrostatic interaction of Cu(II)-ATA greatly contributed to the hydrogen bonding, van der Waals and electrostatic interaction between Cu(II)-ATA and HSA, as confirmed by experimental data. SBIC, 2015 Metallocenter assembly nationallicence Albumin nationallicence Molecular recognition nationallicence Binding affinity nationallicence Docking nationallicence ATA : Aminotriazole nationallicence Cu(II)-ATA : Cu(II)-aminotriazole complex nationallicence CD : Circular dichroism nationallicence FT-IR : Fourier transform infrared spectroscopy nationallicence FRET : Förster's non-radiative energy transfer theory nationallicence HSA : Human serum albumin nationallicence MRE : Mean residue ellipticity nationallicence Yang Lijun College of Chemistry, Liaoning University, 110036, Shenyang, People's Republic of China aut He Lian Shenyang Institute of Geology and Mineral Resources CGS, 110034, Shenyang, People's Republic of China aut Zhang Jing College of Chemistry, Liaoning University, 110036, Shenyang, People's Republic of China aut An Shuai Shenyang Institute of Geology and Mineral Resources CGS, 110034, Shenyang, People's Republic of China aut Zhang Lei College of Chemistry, Liaoning University, 110036, Shenyang, People's Republic of China aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/6(2015-09-01), 1059-1068 0949-8257 20:6<1059 2015 20 775 https://doi.org/10.1007/s00775-015-1287-x text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-015-1287-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Yang Lijun College of Chemistry, Liaoning University, 110036, Shenyang, People's Republic of China aut NATIONALLICENCE 700 1- He Lian Shenyang Institute of Geology and Mineral Resources CGS, 110034, Shenyang, People's Republic of China aut NATIONALLICENCE 700 1- Zhang Jing College of Chemistry, Liaoning University, 110036, Shenyang, People's Republic of China aut NATIONALLICENCE 700 1- An Shuai Shenyang Institute of Geology and Mineral Resources CGS, 110034, Shenyang, People's Republic of China aut NATIONALLICENCE 700 1- Zhang Lei College of Chemistry, Liaoning University, 110036, Shenyang, People's Republic of China aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/6(2015-09-01), 1059-1068 0949-8257 20:6<1059 2015 20 775