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Applied Magnetic Resonance

, Volume 29, Issue 4, pp 703–716 | Cite as

Membrane-peptide interaction studied by PELDOR and CW ESR: Peptide conformations and cholesterol effect on the spatial peptide distribution in the membrane

  • A. D. Milov
  • R. I. Samoilova
  • Yu. D. Tsvetkov
  • F. Formaggio
  • C. Toniolo
  • J. Raap
Article

Abstract

Pulsed electron-electron double resonance (PELDOR) combined with continuous-wave electron paramagnetic resonance was used to study inter- and intramolecular dipole-dipole interactions between spin labels for spin-labeled analogs of trichogin GA IV bound to multilamellar membranes of egg L-α-phosphatidylcholine (ePC) and in ePC membranes containing cholesterol. All samples were frozen to 77 K. For mono-labeled peptide concentrations in lipid over the range between 0.5 to 2.2 mol%, it is shown that in these membranes trichogin molecules are distributed homogeneously and are likely to be located on or near the inner and outer membrane surfaces. Addition of cholesterol to a final concentration of 16.5 mol% leads to an increase of the local concentration of trichogin molecules in the membranes. For the double-labeled trichogin, a distribution of the intramolecular distance between the two spin labels was observed. The distribution function is characterized by two main maxima located at distances of 1.3 and 1.8 nm. The distance of 1.3 nm is close to that expected for the α-helix structure of the peptide chain. The distance of 1.8 nm corresponds to a mixed structure in which a 310-helix is combined with a set of even more elongated conformations.

Keywords

Spin Label Distance Distribution Function Outer Membrane Surface DPPC Membrane PELDOR Signal 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    toniolo C., Crisma M., Formaggio F., Peggion C., Epand R.F., Epand R.M.: Cell. Mol. Life Sci.58, 1179–1188 (2001)CrossRefGoogle Scholar
  2. 2.
    Kropacheva T.N., Raap J.: Biochim. Biophys. Acta1567, 193–203 (2002)CrossRefGoogle Scholar
  3. 3.
    Peggion C., Formaggio F., Crisma M., Epand R.P., Epand R.M., Toniolo C.: J. Pept. Sci.9, 679–689 (2003)CrossRefGoogle Scholar
  4. 4.
    Milov A.D., Samoilova R.I., Tsvetkov Yu.D., Gusev V.A., Formaggio F., Crisma M., Toniolo C., Raap J.: Appl. Magn. Reson.23, 81–95 (2002)CrossRefGoogle Scholar
  5. 5.
    Milov A.D., Erilov D.A., Salnikov E.S., Tsvetkov Yu.D., Formaggio F., Toniolo C., Raap J.: Phys. Chem. Chem. Phys.7, 1794–1799 (2005)CrossRefGoogle Scholar
  6. 6.
    Stella L., Mazzuca C., Venanzi M., Palleschi A., Didonè, Formaggio F., Toniolo C., Pispisa B.: Biophys. J.86, 936–945 (2004)CrossRefADSGoogle Scholar
  7. 7.
    Mazzuca C., Stella L., Venanzi M., Formaggio F., Toniolo C., Pispisa B.: Biophys. J.88, 3411–3421 (2005)CrossRefGoogle Scholar
  8. 8.
    Karle I.L., Balaram P.: Biochemistry29, 6747–6756 (1990)CrossRefGoogle Scholar
  9. 9.
    Toniolo C., Crisma M., Formaggio F., Peggion C.: Biopolymers (Pept. Sci.)60, 396–419 (2001)CrossRefGoogle Scholar
  10. 10.
    Toniolo C., Crisma M., Formaggio F.: Biopolymers (Pept. Sci.)47, 153–158 (1998)CrossRefGoogle Scholar
  11. 11.
    Milov A.D., Salikhov K.M., Shirov M.D.: Fiz. Tverd. Tela (Leningrad)23, 975–982 (1981)Google Scholar
  12. 12.
    Milov A.D., Maryasov A.G., Tsvetkov Yu.D.: Appl. Magn. Reson.15, 107–143 (1998)CrossRefGoogle Scholar
  13. 13.
    Jeschke G., Koch A., Jonas U., Godt A.: J. Magn. Reson.155, 72–82 (2002)CrossRefADSGoogle Scholar
  14. 14.
    Milov A.D., Tsvetkov Yu.D., Formaggio F., Oancea C., Toniolo C., Raap J.: J. Phys. Chem. B107, 13719–13727 (2003)CrossRefGoogle Scholar
  15. 15.
    Jeschke G., Panek G., Godt A., Bender A., Paulsen H.: Appl. Magn. Reson.26, 223–244 (2004)Google Scholar
  16. 16.
    Bowman M.K., Maryasov A.G., Kim N., DeRose V.J.: Appl. Magn. Reson.26, 23–40 (2004)Google Scholar
  17. 17.
    Milov A.D., Naumov B.D., Tsvetkov Yu.D.: Appl. Magn. Reson.26, 587–599 (2004)CrossRefGoogle Scholar
  18. 18.
    Chiang Y.-W., Borbat P.P., Freed J.H.: J. Magn. Reson.172, 279–295 (2005)CrossRefADSGoogle Scholar
  19. 19.
    Monaco V., Formaggio F., Crisma M., Toniolo C., Hanson P., Millhauser G., George C., Deschamps J.R., Flippen-Anderson J.L.: Bioorg. Med. Chem.7, 119–131 (1999)CrossRefGoogle Scholar
  20. 20.
    Monaco V., Formaggio F., Crisma M., Toniolo C., Hanson P., Millhauser G.: Biopolymers50, 239–253 (1999)CrossRefGoogle Scholar
  21. 21.
    Szoka F., Papahadjopoulos D. Jr.: Annu. Rev. Biophys. Bioeng.9, 467–508 (1980)CrossRefGoogle Scholar
  22. 22.
    Milov A.D., Maryasov A.G., Tsvetkov Yu.D., Raap J.: Chem. Phys. Lett.303, 135–143 (1999)CrossRefADSGoogle Scholar
  23. 23.
    Milov A.D., Tsvetkov Yu.D., Formaggio F., Crisma M., Toniolo C., Raap J.: J. Am. Chem. Soc.122, 3843–3848 (2000)CrossRefGoogle Scholar
  24. 24.
    Milov A.D., Tsvetkov Yu.D., Raap J.: Appl. Magn. Reson.19, 215–227 (2000)CrossRefGoogle Scholar
  25. 25.
    Milov A.D., Tsvetkov Yu.D., Formaggio F., Crisma M., Toniolo C., Raap J.: J. Am. Chem. Soc.123, 3784–3789 (2001)CrossRefGoogle Scholar
  26. 26.
    Milov A.D., Tsvetkov Yu.D., Formaggio F., Crisma M., Toniolo C., Raap J.: J. Pept. Sci.9, 690–700 (2003)CrossRefGoogle Scholar
  27. 27.
    Maryasov A.G., Tsvetkov Yu.D.: Appl. Magn. Reson.18, 583 (2000)CrossRefGoogle Scholar
  28. 28.
    Milov A.D., Tsvetkov Yu.D., Formaggio F., Oancea S., Toniolo C., Raap J.: Phys. Chem. Chem. Phys.6, 3596–3603 (2004)CrossRefGoogle Scholar
  29. 29.
    Kutsovsky Y.E., Maryasov A.G., Aristov Y.L., Parmon V.N.: React. Kinet. Catal. Lett.42, 19–24 (1990)CrossRefGoogle Scholar
  30. 30.
    Epand R.F., Epand R.M., Monaco V., Stoia S., Formaggio F., Crisma M., Toniolo C.: Eur. J. Biochem.266, 1021–1028 (1999)CrossRefGoogle Scholar
  31. 31.
    Nagle J.F., Tristram-Nagle S.: Biochim. Biophys. Acta1469, 159–195 (2000)Google Scholar
  32. 32.
    McConnell H.M., Radharishnan A.: Biochim. Biophys. Acta1619, 159–173 (2003)Google Scholar
  33. 33.
    Toniolo C., Benedetti E.: Trends Biochem. Sci.16, 350–353 (1991)CrossRefGoogle Scholar

Copyright information

© Springer 2005

Authors and Affiliations

  • A. D. Milov
    • 1
  • R. I. Samoilova
    • 1
  • Yu. D. Tsvetkov
    • 1
  • F. Formaggio
    • 2
  • C. Toniolo
    • 2
  • J. Raap
    • 3
  1. 1.Institute of Chemical Kinetics and CombustionRussian Academy of SciencesNovosibirskRussian Federation
  2. 2.Institute of Biomolecular Chemistry, Consiglio Nazionale delle Ricerche, Department of ChemistryUniversity of PadovaPadovaItaly
  3. 3.Leiden Institute of Chemistry, Gorlaeus LaboratoriesLeiden UniversityLeidenThe Netherlands

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