title: The interaction between ionic liquids modified magnetic nanoparticles and bovine serum albumin and the cytotoxicity to HepG-2 cells.
abstract: The interaction between ionic liquids modified magnetic Fe3O4 (Fe2) and bovine serum albumin (BSA) is reported and is compared with NH2 functionalized magnetic nanoparticles Fe3O4 (Fe1) based on the UV-visible spectrum, steady-state fluorescence measurements, synchronous fluorescence and DSC methods. The results indicate a static quenching mechanism operating in both nanoparticles. The binding constant of the Fe2-BSA complex calculated from fluorescence data shows that BSA has a low binding affinity for Fe2 than Fe1. DSC data reveal that the thermal stability process of BSA in the Fe2-BSA complex is semi-reversible. This demonstrates that the ionic liquid modified magnetic nanoparticles (Fe2) enhance the thermostability of BSA in the range of 20-40°C, and protein attached Fe2 has higher thermal stability than free BSA. Moreover, the in vitro assay results show that Fe2 shows low cytotoxicity to HepG-2 cells.
authors.affiliation: School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang 212013, PR China.
authors.forename: Juan-Juan
authors.initials: JJ
authors.lastname: Xue
authors.affiliation: School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang 212013, PR China. Electronic address: chenqy@ujs.edu.cn.
authors.forename: Qiu-Yun
authors.initials: QY
authors.lastname: Chen
mesh_terms: D000818:Animals; D002417:Cattle; D056945:Hep G2 Cells / Q000187:drug effects*; D006801:Humans; D052578:Ionic Liquids / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity; D058185:Magnetite Nanoparticles / Q000737:chemistry* / Q000633:toxicity; D055550:Protein Stability / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*
chemical_list: D052578:Ionic Liquids; D058185:Magnetite Nanoparticles; D012710:Serum Albumin, Bovine
keywords: BSA; Interaction; Ionic liquid; Magnetic nanoparticle