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Enzymatic Activity Enhancement of Non-Covalent Modified Superoxide Dismutase and Molecular Docking Analysis
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
* Author to whom correspondence should be addressed.
Received: 30 January 2012; in revised form: 21 March 2012 / Accepted: 22 March 2012 / Published: 30 March 2012
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.
Keywords: non-covalent modification; superoxide dismutase; hydroxypropyl-β-cyclo-dextrin; fluorescence intensity; molecular docking
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MDPI and ACS Style
Qiu, Y.-Z.; Huang, Z.-H.; Song, F.-J. Enzymatic Activity Enhancement of Non-Covalent Modified Superoxide Dismutase and Molecular Docking Analysis. Molecules 2012, 17, 3945-3956.
Qiu Y-Z, Huang Z-H, Song F-J. Enzymatic Activity Enhancement of Non-Covalent Modified Superoxide Dismutase and Molecular Docking Analysis. Molecules. 2012; 17(4):3945-3956.
Qiu, Yan-Zi; Huang, Zong-Hua; Song, Fa-Jun. 2012. "Enzymatic Activity Enhancement of Non-Covalent Modified Superoxide Dismutase and Molecular Docking Analysis." Molecules 17, no. 4: 3945-3956.