Next Article in Journal
4-N,N-Dimethylaminopyridine Promoted Selective Oxidation of Methyl Aromatics with Molecular Oxygen
Previous Article in Journal
Synthesis and Biological Evaluation of Novel Benzothiazole-2-thiol Derivatives as Potential Anticancer Agents
Article Menu

Export Article

Open AccessArticle
Molecules 2012, 17(4), 3945-3956; doi:10.3390/molecules17043945

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 / Revised: 21 March 2012 / Accepted: 22 March 2012 / Published: 30 March 2012
View Full-Text   |   Download PDF [679 KB, uploaded 18 June 2014]   |  

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 non-covalent modification; superoxide dismutase; hydroxypropyl-β-cyclo-dextrin; fluorescence intensity; molecular docking
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

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.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top