Abstract
Differential scanning calorimetry (DSC) is a highly sensitive non-perturbing technique for measuring the thermodynamic properties of thermally induced transitions. This technique is particularly useful for the characterization of lipid/protein interactions. This chapter presents an introduction to DSC instrumentation, basic theory, and methods and describes DSC applications for characterizing protein effects on model lipid membranes. Examples of the use of DSC for the evaluation of protein effects on modulation of membrane domains and membrane stability are given.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Privalov PL, Potekhin SA (1986) Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol 131:4–51
Privalov PL, Dragan AI (2007) Microcalorimetry of biological macromolecules. Biophys Chem 126:16–24
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
McElhaney RN (1986) Differential scanning calorimetric studies of lipid-protein interactions in model membrane systems. Biochim Biophys Acta 864:361–421
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
Lewis RN, Mannock DA, McElhaney RN (2007) Differential scanning calorimetry in the study of lipid phase transitions in model and biological membranes: practical considerations. Methods Mol Biol 400:171–195
Biltonen RL, Lichtenberg D (1993) The use of differential scanning calorimetry as a tool to characterize liposome preparations. Chem Phys Lipids 64:129–142
Seddon AM, Curnow P, Booth PJ (2004) Membrane proteins, lipids and detergents: not just a soap opera. Biochim Biophys Acta 1666:105–117
Cruz A, Casals C, Keough KM, Pérez-Gil J (1997) Different modes of interaction of pulmonary surfactant protein SP-B in phosphatidylcholine bilayers. Biochem J 327:133–138
Papahadjopoulos D, Moscarello M, Eylar EH, Isac T (1975) Effects of proteins on thermotropic phase transitions of phospholipid membranes. Biochim Biophys Acta 401:317–335
Sáenz A, Cañadas O, Bagatolli LA, Sánchez-Barbero F, Johnson ME, Casals C (2007) Effect of surfactant protein A (SP-A) on the physical properties and surface activity of KL4-surfactant. Biophys J 92:482–492
Sáenz A, Lopez-Sanchez A, Mojica-Lazaro J, Martinez-Caro L, Nin N, Bagatolli LA, Casals C (2010) Fluidizing effects of C-reactive protein on lung surfactant membranes: protective role of surfactant protein A. FASEB J 24:3662–3673
Cañadas O, García-Verdugo I, Keough KMW, Casals C (2008) SP-A permeabilizes lipopolysaccharide membranes by forming aggregates that extract lipids from the membrane. Biophys J 95:3287–3294
van Zoelen EJ, van Dijck PW, de Kruijff B, Verkleij AJ, van Deenen LL (1978) Effect of glycophorin incorporation on the physico-chemical properties of phospholipid bilayers. Biochim Biophys Acta 514:9–24
Petri WA, Estep TN, Pal R, Thompson TE, Biltonen RL, Wagner RR (1980) Thermotropic behavior of dipalmitoylphosphatidylcholine vesicles reconstituted with the glycoprotein of vesicular stomatitis virus. Biochemistry 19:3088–3091
Boggs JM, Moscarello MA (1978) Dependence of boundary lipid on fatty acid chain length in phosphatidylcholine vesicles containing a hydrophobic protein from myelin proteolipid. Biochemistry 17:5734–5739
Heyn MP, Blume A, Rehorek M, Dencher NA (1981) Calorimetric and fluorescence depolarization studies on the lipid phase transition of bacteriorhodopsin–dimyristoylphosphatidylcholine vesicles. Biochemistry 20:7109–7115
Semin BK, Saraste M, Wikström M (1984) Calorimetric studies of cytochrome oxidase-phospholipid interactions. Biochim Biophys Acta 769:15–22
Freire E, Markello T, Rigell C, Holloway PW (1983) Calorimetric and fluorescence characterization of interactions between cytochrome b5 and phosphatidylcholine bilayers. Biochemistry 22:1675–1680
Gómez-Fernández JC, Goñi FM, Bach D, Restall C, Chapman D (1979) Protein–lipid interactions. A study of (Ca2+−Mg2+)ATPase reconstituted with synthetic phospholipids. FEBS Lett 98:224–228
Plasencia I, Cruz A, Lopez-Lacomba JL, Casals C, Perez-Gil J (2001) Selective labeling of pulmonary surfactant protein SP-C in organic solution. Anal Biochem 296:49–56
Ivanova VP, Makarov IM, Schaffer TE, Heimburg T (2003) Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A. Biophys J 84:2427–2439
Sáenz A, Cañadas O, Bagatolli LA, Johnson ME, Casals C (2006) Physical properties and surface activity of surfactant-like membranes containing the cationic and hydrophobic peptide KL4. FEBS J 273:2515–2527
Joanne P, Galanth C, Goasdoue N, Nicolas P, Sagan S, Lavielle S et al (2009) Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry. Biochim Biophys Acta 1788:1772–1781
Powers JP, Tan A, Ramamoorthy A, Hancock REW (2005) Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes. Biochemistry 44:15504–15513
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
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
Acknowledgments
This work was supported by the Ministerio de Ciencia e Innovación (SAF2009-07810) and Instituto de Salud Carlos III (cibeRES-CB06/06/0002).
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media New York
About this protocol
Cite this protocol
Cañadas, O., Casals, C. (2013). Differential Scanning Calorimetry of Protein–Lipid Interactions. In: Kleinschmidt, J. (eds) Lipid-Protein Interactions. Methods in Molecular Biology, vol 974. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-275-9_4
Download citation
DOI: https://doi.org/10.1007/978-1-62703-275-9_4
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-62703-274-2
Online ISBN: 978-1-62703-275-9
eBook Packages: Springer Protocols