Skip to main content

Advertisement

SpringerLink
Log in

Monitoring methanol-induced protein unfolding by fluorescence anisotropy measurements of covalently labelled rhodamine probe

  • Regular Article
  • Published:
The European Physical Journal D Aims and scope Submit manuscript

Abstract

We describe the use of an extrinsic fluorophore (rhodamine B isothiocyanate) as a versatile probe to measure rotational motions of proteins. To illustrate the usefulness of this probe, we describe the fluorescence anisotropy values of this fluorophore covalently linked to myoglobin protein measured in aqueous solutions of increased methanol content. Methanol-induced unfolding is revealed by the transition from constrained to free rotation of the covalently attached rhodamine B fluorophore.

Graphical abstract

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. J.R. Lakowicz, Principles of Fluorescence Spectroscopy, 3rd edn. (Springer Science+Business Media, LLC, Singapore, 2006)

  2. A.S. Ladokhin, in Encyclopedia of Analytical Chemistry, edited by R.A. Meyers (Wiley, New York, 2000), pp. 5762–5779

  3. T. Ha, T. Enderle, D.F. Ogletree, D.S. Chemla, P.R. Selvin, S. Weiss, Proc. Natl. Acad. Sci. 93, 6264 (1996)

    Article  ADS  Google Scholar 

  4. D. Canet, K. Doering, C.M. Dobson, Y. Dupont, Biophys. J. 80, 1996 (2001)

    Article  Google Scholar 

  5. A. Ghisaidoobe, S. Chung, Int. J. Mol. Sci. 15, 22518 (2014)

    Article  Google Scholar 

  6. A. Hawe, M. Sutter, W. Jiskoot, Pharm. Res. 25, 1487 (2008)

    Article  Google Scholar 

  7. V. LeTilly, C.A. Royer, Biochemistry 32, 7753 (1993)

    Article  Google Scholar 

  8. A. Marczak, Bioelectrochemistry 74, 236 (2009)

    Article  Google Scholar 

  9. S. Weiss, Nat. Struct. Mol. Biol. 7, 724 (2000)

    Article  Google Scholar 

  10. G. Hungerford, J. Benesch, J.F. Mano, R.L. Reis, Photochem. Photobiol. Sci. 6, 152 (2007)

    Article  Google Scholar 

  11. M. Brinkley, Bioconjug. Chem. 3, 2 (1992)

    Article  Google Scholar 

  12. J.C. Kendrew, G. Bodo, H.M. Dintzis, R.G. Parrish, H. Wyckoff, D.C. Phillips, Nature 181, 662 (1958)

    Article  ADS  Google Scholar 

  13. A. Castro-Forero, D. Jiménez, J. López-Garriga, M. Torres-Lugo, J. Appl. Polym. Sci. 107, 881 (2008)

    Article  Google Scholar 

  14. L.F. Mottram, S. Forbes, B.D. Ackley, B.R. Peterson, Beilstein, J. Org. Chem. 8, 2156 (2012)

    Article  Google Scholar 

  15. M. Girod, X. Dagany, R. Antoine, P. Dugourd, Int. J. Mass Spectrom. 308, 41 (2011)

    Article  ADS  Google Scholar 

  16. M. Girod, X. Dagany, V. Boutou, M. Broyer, R. Antoine, P. Dugourd, A. Mordehai, C. Love, M. Werlich, J. Fjeldsted, G. Stafford, Phys. Chem. Chem. Phys. 14, 9389 (2012)

    Article  Google Scholar 

  17. A. Soleilhac, X. Dagany, P. Dugourd, M. Girod, R. Antoine, Anal. Chem. 87, 8210 (2015)

    Article  Google Scholar 

  18. A. Soleilhac, M. Girod, P. Dugourd, B. Burdin, J. Parvole, P.-Y. Dugas, F. Bayard, E. Lacôte, E. Bourgeat-Lami, R. Antoine, Langmuir 32, 4052 (2016)

    Article  Google Scholar 

  19. D.M. Jameson, J.A. Ross, Chem. Rev. 110, 2685 (2010)

    Article  Google Scholar 

  20. D. Lavalette, C. Tétreau, M. Tourbez, Y. Blouquit, Biophys. J. 76, 2744 (1999)

    Article  Google Scholar 

  21. M.T. Tyn, T.W. Gusek, Biotechnol. Bioeng. 35, 327 (1990)

    Article  Google Scholar 

  22. S.Z. Mikhail, W.R. Kimel, J. Chem. Eng. Data 6, 533 (1961)

    Article  Google Scholar 

  23. T.T. Herskovits, B. Gadegbeku, H. Jaillet, J. Biol. Chem. 245, 2588 (1970)

    Google Scholar 

  24. Q. Shao, J. Phys. Chem. B 118, 6175 (2014)

    Article  Google Scholar 

  25. A. Fernández, O. Sinanoglu, Biophys. Chem. 21, 163 (1985)

    Article  Google Scholar 

  26. J. Seo, W. Hoffmann, S. Warnke, M.T. Bowers, K. Pagel, G. von Helden, Angew. Chem. Int. Ed. 55, 14173 (2016)

    Article  Google Scholar 

  27. Y.Y. Gottlieb, P. Wahl, J. Chim. Phys. Phys. Chim. Biol. 60, 849 (1963)

    Article  Google Scholar 

  28. K. Kinosita, S. Kawato, A. Ikegami, Biophys. J. 20, 289 (1977)

    Article  Google Scholar 

  29. G.F. Schröder, U. Alexiev, H. Grubmüller, Biophys. J. 89, 3757 (2005)

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institut lumière matière, UMR5306 Université Claude Bernard Lyon1-CNRS, Université de Lyon, 69622, Villeurbanne Cedex, France

    Antonin Soleilhac, Franck Bertorelle, Philippe Dugourd & Rodolphe Antoine

  2. Univ Lyon, CNRS, Université Claude Bernard Lyon 1, Ens de Lyon, Institut des Sciences Analytiques, UMR 5280, 5 rue de la Doua, 69100, Villeurbanne, France

    Marion Girod

Authors
  1. Antonin Soleilhac
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Franck Bertorelle
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Philippe Dugourd
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Marion Girod
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Rodolphe Antoine
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Rodolphe Antoine.

Additional information

Contribution to the Topical Issue “Dynamics of Systems at the Nanoscale”, edited by Andrey Solov’yov and Andrei Korol.

Supplementary material in the form of one pdf file available from the Journal web page at https://doi.org/10.1140/epjd/e2017-70760-3

Electronic supplementary material

Supplementary data

PDF file

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Soleilhac, A., Bertorelle, F., Dugourd, P. et al. Monitoring methanol-induced protein unfolding by fluorescence anisotropy measurements of covalently labelled rhodamine probe. Eur. Phys. J. D 71, 142 (2017). https://doi.org/10.1140/epjd/e2017-70760-3

Download citation

  • Received:

  • Revised:

  • Published:

  • DOI: https://doi.org/10.1140/epjd/e2017-70760-3

Search

Navigation