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Journal of Applied Spectroscopy

, Volume 83, Issue 1, pp 149–155 | Cite as

Study of Ellagic Acid as a Natural Elastase Inhibitor by Spectroscopic Methods

  • X. Xing
  • X. Yang
  • Yu. Cao
Article
  • 53 Downloads

A new natural inhibitor, ellagic acid (EA), was developed, and its inhibition efficiency on elastase was studied by spectroscopic methods. The experimental results proved that EA is a potent elastase inhibitor with an IC50 value of 1.44 mg/mL by UV-vis spectroscopy, and the inhibition mechanism of elastase was confirmed by fluorescence quenching. The interacting between EA and elastase was mainly based on the static quenching owing to the complex formation when the concentration of EA was ≤40 μM. Fluorescence quenching mainly occurred via dynamic quenching with increasing EA concentration. The thermodynamic parameters such as ΔH and ΔS were calculated to be –86.35 kJ/mol and –165.88 J/mol · K, respectively, indicating that the interactions between EA and elastase were mainly due to van der Waals forces or hydrogen bonding. The synchronous fl uorescence spectra showed that binding of EA to elastase can induce conformational changes in elastase.

Keywords

spectroscopy ellagic acid elastase inhibition mechanism 

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Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  1. 1.Yancheng Institute of TechnologyYanchengChina
  2. 2.School of Chemical and Material EngineeringJiangnan UniversityWuxiChina

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