Multispectral and molecular modeling investigations on the binding behaviors of two anticoccidials with serum albumins. Issue 14 (22nd September 2022)

• Record Type: Journal Article
• Authors: Li, Xu; Zhao, Rui; Shao, Di; Yuan, Yue; Bi, Shuyun
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 40:Issue 14(2022)
• Page Start: 6522
• Page End: 6533
• Publication Date: 2022-09-22
• Subjects: Monensin -- clopidol -- serum albumins -- multispectral -- molecular modeling; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2021.1886173
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract: The interaction properties of monensin/clopidol with bovine/human serum albumin (BSA/HSA) were determined via multispectral together with molecular modeling techniques in the report. Fluorescence quenching spectra at different temperatures and fluorescence lifetime determination demonstrated that the fluorescence quenching belonged to a static quenching type. In the case of monensin-BSA, clopidol-BSA, monensin-HSA and clopidol-HSA, the binding constants K a (291 K) were 5.42 × 10 4, 4.96 × 10 4, 3.22 × 10 4 and 2.99 × 10 4 M −1, respectively; the binding distances r 0 were 1.88, 2.53, 2.19 and 2.02 nm, respectively. Monensin and clopidol bound strongly with BSA/HSA with binding free energies equal to −26.37/−25.11 and −26.11/−24.93 kJ mol −1, respectively. The spontaneous binding process was dominated by hydrogen bonds and van der Waals forces as reflected in thermodynamic parameters analyses. Synchronous, CD, FTIR and UV-vis spectra assays confirmed that serum albumins conformations were altered. Using competitive experiment, monensin/clopidol was observed to bind at site I of serum albumins, which were reconfirmed by the results of molecular modeling. Communicated by Ramaswamy H. Sarma Abstract : UF0001