Abstract
This chapter addresses the determination of protein–lipid selectivity, here described as the preference of a protein for having a specific type of lipid in its vicinity (annular lipids), from Förster resonance energy transfer methodologies. These allow a quantification of the effect, i.e., the determination of the biasing in distribution of the lipid under study around the protein, as compared to its bulk membrane distribution, with advantages over established approaches that have been used for the same purpose, such as electron spin resonance spectroscopy. The experiment can be carried out with steady-state instrumentation, the formalisms are described in detail, and the model can be applied to a membrane protein of any size.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Marsh D (2008) Electron spin resonance in membrane research: protein-lipid interactions. Methods 46:83–96
Nyholm TK, Ozdirekcan S, Killian JA (2007) How protein transmembrane segments sense the lipid environment. Biochemistry 46:1457–1465
Czech MP (2000) PIP2 and PIP3: complex roles at the cell surface. Cell 100:603–606
Lee AG (2003) Lipid–protein interactions in biological membranes: a structural perspective. Biochim Biophys Acta 1612:1–40
Marsh D, Horváth LI (1998) Structure, dynamics and composition of the lipid–protein interface. Perspectives from spin-labeling. Biochim Biophys Acta 1376:267–296
London E, Feigenson GW (1981) Fluorescence quenching in model membranes. 1. Characterization of quenching by a spin-labeled phospholipid. Biochemistry 20:1932–1938
Everett J, Zlotnick A, Tennyson J, Holloway PW (1986) Fluorescence quenching of cytochrome b5 in vesicles with an asymmetric transbilayer distribution of brominated phosphatidylcholine. J Biol Chem 261:6725–6729
Förster T (1949) Experimentelle und theoretische Untersuchung des Zwischenmolekularen übergangs von Elektrinenanregungsenergie. Z Naturforsch 4a:321–327
Van Der Meer B, Coker V III, Chen S-YS (1994) Resonance energy transfer: theory and data. VCH Publishers, New York
Fernandes F, Loura LMS, Koehorst R, Spruijt RB, Hemminga MA, Fedorov A, Prieto M (2004) Quantification of protein-lipid selectivity using FRET: application to the M13 major coat protein. Biophys J 87:344–352
Fung BK, Stryer L (1978) Surface density determination in membranes by fluorescence energy transfer. Biochemistry 17:5241–5248
Wolber PK, Hudson BS (1979) An analytical solution to the Förster energy transfer problem in two dimensions. Biophys J 28:197–210
Spruijt RB, Wolfs CJ, Verver JW, Hemminga MA (1996) Accessibility and environment probing using cysteine residues introduced along the putative transmembrane domain of the major coat protein of bacteriophage M13. Biochemistry 35:10383–10391
Picas L, Suárez-Germà C, Montero MT, Vázquez-Ibar JL, Hernández-Borrell J, Prieto M, Loura LM (2010) Lactose permease lipid selectivity using Förster resonance energy transfer. Biochim Biophys Acta 1798:1707–1713
Lakowicz JR (2006) Principles of fluorescence spectroscopy, 3rd edn. Kluwer Academic/Plenum, New York
Davenport L et al (1985) Transverse location of the fluorescent probe 1,6-diphenyl-1,3,5-hexatriene in model lipid bilayer membrane systems by resonance energy transfer. Biochemistry 24:4097–4108
Loura LMS, Fedorov A, Prieto M (1996) Resonance energy transfer in a model system of membranes: application to gel and liquid crystalline phases. Biophys J 71:1823–1836
Koehorst RBM, Spruijt RB, Vergeldt FJ, Hemminga MA (2004) Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy. Biophys J 87:1445–1455.
Acknowledgments
F.F. acknowledges a research grant (SFRH/BPD/64320/2009) from Fundacão para a Ciência e Tecnologia (FCT). F.F., M.P., and L.M.S.L. acknowledge funding by FEDER (COMPETE program), and by FCT (Fundação para a Ciência e a Tecnologia), project references PTDC/QUI-BIQ/112067/2009, PTDC/QUI-BIQ/099947/2008, and FCOMP-01-0124-FEDER-010787 (FCT PTDC/QUI-QUI/098198/2008).
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
Loura, L.M.S., Prieto, M., Fernandes, F. (2013). Förster Resonance Energy Transfer as a Tool for Quantification of Protein–Lipid Selectivity. 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_10
Download citation
DOI: https://doi.org/10.1007/978-1-62703-275-9_10
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