Affiliation

Key Laboratory of Analytical Science and Technology of Hebei Province, College of Chemistry & Environmental Science, Hebei University, Baoding 071002, Hebei Province, P. R. China

Corresponding Author

Baosheng Liu, Key Laboratory of Analytical Science and Technology of Hebei Province, College of Chemistry & Environmental Science, Hebei University, Baoding 071002, Hebei Province, P. R. China, Tel: +86-312-5079385, Fax: +86-312-5079525; E-mail: lbs@hbu.edu.cn

Citation

Liu, B., et al. Spectroscopy and Molecular Docking Analysis of the Interaction between Trypsin and Cefpirome. (2017) J Anal Bioanal Sep Tech 2(1): 67- 74.

Copy rights

© 2017 Liu, B. Sams. This is an Open access article distributed under the terms of Creative Commons Attribution 4.0 International License.

Keywords

Abstract

  The interaction between Cefpirome and Trypsin was studied using multi-spectroscopy and molecular docking methods. The results showed that quenching mechanism of the Trypsin-Cefpirome system was probably static. The main interaction force was electrostatic force, and the number of binding sites in this system was approximately equal to 1. The quenching curves indicated that the tyrosine and tryptophan residues were both involved in the reaction. Synchronous fluorescence spectroscopy further confirmed that the main binding site was closer to tryptophan residues. The distance (r) between Trypsin and Cefpirome was less than 7 nm, which indicated that the energy transfer from Trypsin to Cefpirome was non-radiative energy transfer. The values of the Hill’s coefficients showed that there was negative cooperativity in the interaction between Cefpirome and Trypsin.