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Interaction of TiO2 nanoparticle with trypsin analyzed by kinetic and spectroscopic methods

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Abstract

In this study, the stability and structure of bovine pancreas trypsin against TiO2 nanoparticle have investigated through thermal stability, fluorescence and circular dichroism spectroscopy, and enzyme activity assay. The enzyme activity of trypsin showed that TiO2 nanoparticles compound inhibited the activity of the enzyme non-competitively. The inhibition constant K i value was calculated to be 29 µM (310 K). Thermal stability was decreased from 318 to 314.2 K by enhancing the concentration of nanoparticles. Far-UV circular dichroism studies showed that TiO2 nanoparticles could change the secondary structure of trypsin via a decrease in the content of α-helix structure (0.3 %) and an increase in the β-sheet (1.5 %). The Stern–Volmer constant decreases from 4.8 × 108 to 4.0 × 108 M−1 by increasing temperature from 298 to 308 K. It was observed that TiO2 nanoparticle quenched the intrinsic fluorescence of trypsin by the static quenching mechanism. The thermodynamic parameters also indicated that the binding process was spontaneous, in which electrostatic interaction played an important role in the interaction of TiO2 nanoparticles with trypsin.

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Acknowledgments

The work was financially helped via the University of Shahrekord, Iran. The authors also thank the University of Tehran for helping in CD experiments.

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Authors and Affiliations

  1. Department of Biology, Faculty of Science, University of Shahrekord, P. O. Box.115, Shahrekord, Iran

    L. Momeni & Behzad Shareghi

  2. Department of Biology, Faculty of Science, University of Payam Noor, Tehran, Iran

    L. Momeni

  3. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

    A. A. Saboury & M. Evini

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  1. L. Momeni
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  2. Behzad Shareghi
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  3. A. A. Saboury
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  4. M. Evini
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Correspondence to Behzad Shareghi.

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Momeni, L., Shareghi, B., Saboury, A.A. et al. Interaction of TiO2 nanoparticle with trypsin analyzed by kinetic and spectroscopic methods. Monatsh Chem 148, 199–207 (2017). https://doi.org/10.1007/s00706-016-1772-0

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  • DOI: https://doi.org/10.1007/s00706-016-1772-0

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