Binding study of florfenicol with DNA by multi-spectroscopy and molecular docking techniques. (September 2021)

• Record Type: Journal Article
• Authors: Li, Xu; Yuan, Yue; Wang, Yuting; Zhang, Fengming; Zhao, Rui; Shao, Di; Bi, Shuyun
• Is Part Of: Process biochemistry. Volume 108(2021)
• Page Start: 26
• Page End: 33
• Publication Date: 2021-09
• Subjects: Florfenicol -- DNA -- Minor groove -- Multi-spectroscopy -- Molecular docking; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2021.05.023
• Languages: English
• ISSNs: 1359-5113

Abstract

Graphical abstract: Highlights: The binding of residual florfenicol in animal-derived food and DNA was studied. The interaction information was obtained by multispectral techniques. Molecular docking simulated the binding mode of DNA to ligand. Florfenicol was a minor groove binder of DNA. Abstract: The investigation on the binding interaction mechanism of florfenicol with DNA in vitro was reported via multi-spectroscopy measurements and molecular docking approach in the present work. The static fluorescence quenching process accompanied with non-radiation energy transfer between florfenicol and DNA was confirmed by Stern-Volmer analysis, lifetime measurement and fluorescence resonance energy transfer study. Florfenicol was the A-T rich minor groove binding agent of DNA. Various experiments including site marker competitive experiments, viscosity measurements, helix melting studies, ionic strength measurements, thermal denaturation experiments, circular dichroism (CD) spectra measurements and UV–vis spectra characteristics were carried out to disclose the interaction mode. In addition, molecular docking stimulated appropriate binding orientation to further prove above experimental results. The binding constants were 6.92 × 10 3, 6.21 × 10 3 and 5.61 × 10 3 M −1 at 291, 301 and 311 K respectively and the binding distance r 0 was 5.30 nm. Thermodynamic parameters, such as Δ H Ө =−7.90 kJ mol −1 and Δ S Ө = 46.39 J mol −1 K −1, showed that electrostatic attraction was the key force in the binding.