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Fluorescence Spectroscopy as a Tool to Unravel the Dynamics of Protein Nanoparticle Formation by Liquid Antisolvent Precipitation

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Abstract

Protein-based particles are very promising colloidal systems for protection and controlled release applications in the food, cosmetics and pharmaceutical sector. One technique to produce these protein colloidal particles is liquid antisolvent precipitation (LAS). Despite the simplicity and versatility of LAS, not much is known about the protein conformational changes and interactions that are at the basis of the particle formation process. In this study, steady state fluorescence experiments using intrinsic fluorophores were evaluated as a tool to unravel the dynamics of the protein nanoparticle formation. Colloidal whey protein isolate and gliadin particles were produced by LAS. Changes in particle diameter (distribution), polydispersity index and photophysical properties of intrinsic fluorophores were monitored as a function of antisolvent concentration. By combining dynamic light scattering with photophysical data, a model of the changes occurring during particle formation and disintegration could be proposed. The results suggest that particle formation and disintegration are fully reversible processes during which the main changes in protein conformation (around the fluorescent probes) occur at the same antisolvent concentrations. In principle, steady state fluorescence measurements using intrinsic probes can indeed be used to effectively report on (part of the) conformational changes for both protein systems under study.

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Abbreviations

DLS:

dynamic light scattering

LAS:

liquid antisolvent precipitation

RET:

resonance energy transfer

WPI:

whey protein isolate

References

  1. I.J. Joye, Curr. Top. Med. Chem. 16(9), 1026–1039 (2016)

    Article  CAS  Google Scholar 

  2. I.J. Joye, D.J. McClements, Curr. Opin. Colloid Interface Sci. 19(5), 417–427 (2014)

    Article  CAS  Google Scholar 

  3. A. Mitra, L. Li, P. Marsac, B. Marks, Z. Liu, C. Brown, Int. J. Pharm. 505(1–2), 107–114 (2016)

    Article  CAS  Google Scholar 

  4. S.R. Yearla, K. Padmasree, J. Exp, Nano 11(4), 289–302 (2016)

    CAS  Google Scholar 

  5. I.J. Joye, D.J. McClements, Trends Food Sci. Technol. 34(2), 109–123 (2013)

    Article  CAS  Google Scholar 

  6. K. Langer, S. Balthasar, V. Vogel, N. Dinauer, H. von Brieesn, D. Schubert, Int. J. Pharm. 257(1–2), 169–180 (2003)

    Article  CAS  Google Scholar 

  7. B. Subia, S.C. Kundu, Nanotechnology 24(3), 1–11 (2013)

    Article  Google Scholar 

  8. A.R. Patel, E.C.M. Bouwens, K.P. Velikov, J. Agric, Food Chem. 58(23), 12497–12503 (2010)

    Article  CAS  Google Scholar 

  9. A.A. Thorat, S.V. Dalvi, Chem. Eng. J. 181-182, 1–34 (2012)

    Article  CAS  Google Scholar 

  10. C.A. Royer, Chem. Rev. 106, 1769–1784 (2006)

    Article  CAS  Google Scholar 

  11. J.R. Lakowicz, Principles of fluorescence spectroscopy, 3rd edn. (Springer Science+Business Media, New York, 2006), 923 p

    Book  Google Scholar 

  12. M.R. Eftink, Biophys. J. 66, 482–501 (1994)

    Article  CAS  Google Scholar 

  13. E. Lanzarotti, R.R. Biekofsky, D.A. Estrin, M.A. Marti, A.G. Turjanski, J. Chem, Inf. Model. 51(7), 1623–1633 (2011)

    Article  CAS  Google Scholar 

  14. AOAC, (Association of Official Analytical Chemists, WA, 1995)

  15. M. Peleg, M.G. Corradini, M.D. Normand, Chem. Ing. Tech. 76, 413–423 (2004)

    Article  CAS  Google Scholar 

  16. I.S. Khattab, F. Bandarkar, M.A.A. Fakhree, A. Jouyban, Korean J. Chem. Eng. 29(6), 812–817 (2011)

    Article  Google Scholar 

  17. P.L.H. McSweeney and P.F. Fox, Advanced Dairy Chemistry Vol. 1A: Proteins: Basic Aspects, 4th edn. (Springer, NY, 2013), 538 p

  18. H.M. Hudson, C.R. Daubert, E.A. Foegeding, J. Agric, Food Chem. 48(8), 3112–3119 (2000)

    Article  CAS  Google Scholar 

  19. S. Ang, J. Kogulanathan, G.A. Morris, et al., Eur. Biophys. J. 39, 255–261 (2010)

    Article  CAS  Google Scholar 

  20. J.T. Vivian, P.R. Callis, Biophys. J. 80, 2093–2109 (2001)

    Article  CAS  Google Scholar 

  21. Z.Y. Ju, A. Kilara, J. Agric, Food Chem. 46, 1830–1835 (1998)

    Article  CAS  Google Scholar 

  22. M.L. Quillin, B.W. Matthews, Acta Crystallogr. Sect. D 56(7), 791–794 (2000)

    Article  CAS  Google Scholar 

  23. N. Hirota-Nakaoka, Y. Goto, Bioorg. Med. Chem. 7, 67–73 (1999)

    Article  CAS  Google Scholar 

  24. S. Shimizu, K. Shimizu, J. Am, Chem. Soc. 121, 2387–2394 (1999)

    Article  CAS  Google Scholar 

  25. P.R. Callis, J. Mol, Structure 1077, 22–29 (2014)

    CAS  Google Scholar 

  26. Y. Chen, M.D. Barkley, Biochemistry 37, 9976–9982 (1998)

    Article  CAS  Google Scholar 

  27. B. Valeur, G. Weber, Photochem. Photobiol. 25, 441–444 (1977)

    Article  CAS  Google Scholar 

  28. M. Wojdyr, J. Appl, Crystallogr. 43, 1126–1128 (2010)

    Article  CAS  Google Scholar 

  29. J.R. Lakowicz, B. Kierdaszuk, P.R. Callis, H. Malak, I. Gryczynski, Biophys. Chem. 5, 263–271 (1995)

    Article  Google Scholar 

Download references

Acknowledgements

Iris Joye gratefully acknowledges financial support from the ‘Fonds voor Wetenschappelijk Onderzoek – Vlaanderen’ (FWO, Brussels, Belgium) and from the European Commission 7th Framework Program (FP7-People-2011-IOF-300408). Richard D. Ludescher would like to acknowledge the support of the Agriculture and Food Research Initiative Grant no. 2013-67017-21649 from the USDA National Institute of Food and Agriculture, Improving Food Quality –A1361.

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Authors and Affiliations

  1. Department of Food Science, Rutgers, The State University of New Jersey, New Brunswick, NJ, USA

    Maria G. Corradini & Richard D. Ludescher

  2. Department of Food Science, University of Massachusetts, Amherst, MA, USA

    Maria G. Corradini

  3. Department of Microbial and Molecular Systems, KU Leuven, Heverlee, Belgium

    Maarten Demol, Jeroen Boeve & Iris J. Joye

  4. Department of Food Science, University of Guelph, Guelph, Canada

    Iris J. Joye

Authors
  1. Maria G. Corradini
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  2. Maarten Demol
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  3. Jeroen Boeve
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  4. Richard D. Ludescher
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  5. Iris J. Joye
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Correspondence to Iris J. Joye.

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Corradini, M.G., Demol, M., Boeve, J. et al. Fluorescence Spectroscopy as a Tool to Unravel the Dynamics of Protein Nanoparticle Formation by Liquid Antisolvent Precipitation. Food Biophysics 12, 211–221 (2017). https://doi.org/10.1007/s11483-017-9477-4

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  • DOI: https://doi.org/10.1007/s11483-017-9477-4

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