title: Enzymatic activity enhancement of non-covalent modified superoxide dismutase and molecular docking analysis.
abstract: The enzyme activity of superoxide dismutase was improved in the pyrogallol autoxidation system by about 27%, after interaction between hydroxypropyl-β-cyclo-dextrin and superoxide dismutase. Fluorescence spectrometry was used to study the interaction between hydroxypropyl-β-cyclodextrin and superoxide dismutase at different temperatures. By doing this, it can be found that these interactions increase fluorescence sensitivity. In the meantime, the synchronous fluorescence intensity revealed the interaction sites to be close to the tryptophan (Trp) and tyrosine (Tyr) residues of superoxide dismutase. Furthermore, molecular docking was applied to explore the binding mode between the ligands and the receptor. This suggested that HP-β-CD interacted with the B ring, G ring and the O ring and revealed that the lysine (Lys) residues enter the nanocavity. It was concluded that the HP-β-CD caused specific conformational changes in SOD by non-covalent modification.
authors.affiliation: College of Life Science/Key Laboratory for Biotechnology of the State Ethnic Affairs Commission, South Central University for Nationalities, 708 Minyuan Road, Wuhan 430074, China. qiuyan862724@163.com
authors.forename: Yan-Zi
authors.initials: YZ
authors.lastname: Qiu
authors.forename: Zong-Hua
authors.initials: ZH
authors.lastname: Huang
authors.forename: Fa-Jun
authors.initials: FJ
authors.lastname: Song
mesh_terms: D000495:Allosteric Site; D003198:Computer Simulation; D004789:Enzyme Activation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013482:Superoxide Dismutase / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D013482:Superoxide Dismutase