FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (21): 165-168.doi: 10.7506/spkx1002-6630-201021037

• Basic Research • Previous Articles     Next Articles

Effect of Sudan Red III on Fluorescence Quenching of Myoglobin and Molecular Modeling of Their Interaction

ZHU Shao-ping1,CAI Bing-feng2,MAO Hui2,ZHAO Bo2,*   

  1. 1. School of Science, Changzhou Institute of Technology, Changzhou 213002, China;2. Jiangsu Key Laboratory of Biofunctional
    Materials, College of Chemistry and Materials Science, Nanjing Normal University, Nanjing 210097, China
  • Received:2010-08-03 Online:2010-11-15 Published:2010-12-29
  • Contact: ZHAO Bo2 E-mail:zhaobo@njnu.edu.cn

Abstract:

The molecular interaction mechanism between Sudan red III and myoglobin (Mb) was investigated by fluorescence spectrum combined with molecular modeling under the mimic physiological conditions. Results showed that the fluorescence of Mb was quenched by Sudan red III due to the complex formation between them. This kind of fluorescence quenching was a static quenching. Molecular modeling revealed that Sudan red III could bind to the Site 1 of Mb. Hydrophobic interaction and hydrogen bond formation contribute to the binding of Sudan red III. The hydrophobic interaction and hydrophilic interaction between Sudan red III and Trp, Tyr, Phe residues in Mb resulted in static fluorescence quenching of Mb and disordered displacement of maximum emission peak. These interactions were focused on the residues of Phe33, Phe43 and Phe138 in Mb.

Key words: Sudan red III, myoglobin, interaction, fluorescence quenching, molecular modeling

CLC Number: