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Lipid-Protein Interactions pp 91–106Cite as

Differential Scanning Calorimetry of Protein–Lipid Interactions

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 2003))

Abstract

Differential scanning calorimetry (DSC) is a highly sensitive nonperturbing technique used for studying the thermodynamic properties of thermally induced transitions. Since these properties might be affected by ligand binding, DSC is particularly useful for the characterization of protein interactions with biomimetic membranes. The advantages of this technique over other methods consist in the direct measurement of intrinsic thermal properties of the samples, requiring no chemical modifications or extrinsic probes. This chapter describes the basic theory of DSC and provides the reader with an understanding of the capabilities of DSC instrumentation and the type of information that can be achieved from DSC studies of lipid–protein interactions. In particular, the chapter provides a detailed analysis of DSC data to assess the effects of proteins on biomimetic membranes.

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References

  1. McElhaney RN (1982) The use of differential scanning calorimetry and differential thermal analysis in studies of model and biological membranes. Chem Phys Lipids 30:229–259

    Article  CAS  Google Scholar 

  2. McElhaney RN (1986) Differential scanning calorimetric studies of lipid-protein interactions in model membrane systems. Biochim Biophys Acta 864:361–421

    Article  CAS  Google Scholar 

  3. Demetzos C (2008) Differential scanning calorimetry (DSC): a tool to study the thermal behavior of lipid bilayers and liposome stability. J Liposome Res 18:159–173

    Article  CAS  Google Scholar 

  4. Lewis RN, Mannock DA, McElhaney RN (2007) Differential scanning calorimetry in the study of lipid phase transitions in model and biological membranes. In: Dopico AM (ed) Methods in membrane lipids. Methods in molecular biology™, vol 400. Humana Press, Totowa, NJ, pp 171–195

    Google Scholar 

  5. Biltonen RL, Lichtenberg D (1993) The use of differential scanning calorimetry as a tool to characterize liposome preparations. Chem Phys Lipids 64:129–142

    Article  CAS  Google Scholar 

  6. Niebylski CD, Salem NJ (1994) A calorimetric investigation of a series of mixed-chain polyunsaturated phosphstidylcholines: effect of sn-2 chain length and degree of unsaturation. Biophys J 67:2387–2393

    Article  CAS  Google Scholar 

  7. Naghibi H, Tamura A, Sturtevant JM (1995) Significant discrepancies between van’t Hoff and calorimetric enthalpies. Proc Natl Acad Sci U S A 92:5597–5599

    Article  CAS  Google Scholar 

  8. Seddon AM, Curnow P, Booth PJ (2004) Membrane proteins, lipids and detergents: not just a soap opera. Biochim Biophys Acta 1666:105–117

    Article  CAS  Google Scholar 

  9. Rigaud JL, Pitard B, Levy D (1995) Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins. Biochim Biophys Acta 1231:223–246

    Article  Google Scholar 

  10. Cruz A, Casals C, Keough KM et al (1997) Different modes of interaction of pulmonary surfactant protein SP-B in phosphatidylcholine bilayers. Biochem J 327:133–138

    Article  CAS  Google Scholar 

  11. Privalov PL, Dragan AI (2007) Microcalorimetry of biological macromolecules. Biophys Chem 126:16–24

    Article  CAS  Google Scholar 

  12. Privalov PL, Potekhin SA (1986) Scanning microcalorimetry in studying temperature-induced changes in proteins. In: Hirs C, Timasheff S (eds) Enzyme structure, Part L, vol 131. Academic Press, Orlando, FL, pp 4–51

    Chapter  Google Scholar 

  13. Spink CH (2015) The deconvolution of differential scanning calorimetry unfolding transitions. In: Chaires JB, Hansen LD, Keller S, Brautigam CA, Zhao H, Schuck P (eds) Biocalorimetry. Methods, vol 76. Elsevier, Amsterdam, pp 78–86

    Google Scholar 

  14. Cañadas O, Casals C (2013) Differential scanning calorimetry of protein-lipid interactions. In: Kleinschmidt J (ed) Lipid-protein interactions. Methods in molecular biology (Methods and protocols), vol 974. Humana Press, Totowa, NJ, pp 55–71

    Chapter  Google Scholar 

  15. Papahadjopoulos D, Moscarello M, Eylar EH et al (1975) Effects of proteins on thermotropic phase transitions of phospholipid membranes. Biochim Biophys Acta 401:317–335

    Article  CAS  Google Scholar 

  16. van Zoelen EJ, van Dijck PW, de Kruijff B et al (1978) Effect of glycophorin incorporation on the physico-chemical properties of phospholipid bilayers. Biochim Biophys Acta 514:9–24

    Article  Google Scholar 

  17. Gómez-Fernández JC, Goñi FM, Bach D et al (1979) Protein—lipid interactions. A study of (Ca2+-Mg2+)ATPase reconstituted with synthetic phospholipids. FEBS Lett 98:224–228

    Article  Google Scholar 

  18. Poveda JA, Fernández AM, Encinar JA et al (2008) Protein-promoted membrane domains. Biochim Biophys Acta 1778:1583–1590

    Article  CAS  Google Scholar 

  19. Sáenz A, Cañadas O, Bagatolli LA et al (2006) Physical properties and surface activity of surfactant-like membranes containing the cationic and hydrophobic peptide KL4. FEBS J 273:2515–2527

    Article  Google Scholar 

  20. Plasencia I, Cruz A, Lopez-Lacomba JL et al (2001) Selective labeling of pulmonary surfactant protein SP-C in organic solution. Anal Biochem 296:49–56

    Article  CAS  Google Scholar 

  21. Siegel DP, Epand RM (1997) The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: implications for membrane fusion mechanisms. Biophys J 73:3089–3111

    Article  CAS  Google Scholar 

  22. White SH, Wimley WC (1999) Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct 28:319–365

    Article  CAS  Google Scholar 

  23. Mason JT, Huang CM, Biltonen RL (1983) Effect of liposomal size on the calorimetric behavior of mixed-chain phosphatidylcholine bilayers dispersions. Biochemistry 22:2013–2018

    Article  CAS  Google Scholar 

  24. Shaw AW, McLean MA, Sligar SG (2004) Phospholipid phase transitions in homogeneous nanometer scale bilayer discs. FEBS Lett 556:260–264

    Article  CAS  Google Scholar 

  25. Haynie DT, Freire E (1994) Estimation of the folding/unfolding energetics of marginally stable proteins using differential scanning calorimetry. Anal Biochem 216:33–41

    Article  CAS  Google Scholar 

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Acknowledgments

This work was supported by Spanish Ministry of Economy and Competitiveness (SAF2015-65307-R) and Institute of Health Carlos III (CIBERES CB06/06/0002).

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Faculty of Chemistry, Complutense University of Madrid, Madrid, Spain

    Olga Cañadas & Cristina Casals

  2. Centro de Investigación Biomédica en Red de Enfermedades Respiratorias (CIBERES), Instituto de Salud Carlos III, Madrid, Spain

    Olga Cañadas & Cristina Casals

Authors
  1. Olga Cañadas
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  2. Cristina Casals
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Corresponding author

Correspondence to Cristina Casals .

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Editors and Affiliations

  1. Department of Biophysics, Institute of Biology, FB10 and Center for Interdisciplinary Nanostructure Science and Technology (CINSaT), University of Kassel, Kassel, Germany

    Jörg H. Kleinschmidt

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Cañadas, O., Casals, C. (2019). Differential Scanning Calorimetry of Protein–Lipid Interactions. In: Kleinschmidt, J. (eds) Lipid-Protein Interactions. Methods in Molecular Biology, vol 2003. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9512-7_5

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  • DOI: https://doi.org/10.1007/978-1-4939-9512-7_5

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-4939-9511-0

  • Online ISBN: 978-1-4939-9512-7

  • eBook Packages: Springer Protocols

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