Abstract
Surface plasmon resonance (SPR) is an established method for studying molecular interactions in real time. It allows obtaining qualitative and quantitative data on interactions of proteins with lipids or lipid membranes. In most of the approaches a lipid membrane or a membrane-mimetic surface is prepared on the surface of Biacore (GE Healthcare) sensor chips HPA or L1, and the studied protein is then injected across the surface. Here we provide an overview of SPR in protein–lipid and protein–membrane interactions, different approaches described in the literature and a general protocol for conducting an SPR experiment including lipid membranes, together with some experimental considerations.
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References
Rich RL, Myszka DG (2010) Grading the commercial optical biosensor literature-class of 2008: ‘The Mighty Binders’. J Mol Recognit 23:1–64
Rich RL, Myszka DG (2011) Survey of the 2009 commercial optical biosensor literature. J Mol Recognit 24:892–914
Schasfoort RBM (ed) (2017) Handbook of surface plasmon resonance. The Royal Society of Chemistry, Mabridge
de Mol NJ, Fischer MJE (eds) (2008) Surface plasmon resonance: methods and protocols. Humana Press, New York, NY
Beseničar M, Maček P, Lakey JH, Anderluh G (2006) Surface plasmon resonance in protein–membrane interactions. Chem Phys Lipids 141:169–178
Cho W, Bittova L, Stahelin RV (2001) Membrane binding assays for peripheral proteins. Anal Biochem 296:153–161
Cooper MA (2004) Advances in membrane receptor screening and analysis. J Mol Recognit 17:286–315
Stahelin RV (2013) Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions. Mol Biol Cell 24:883–886
Stenberg E, Persson B, Roos H, Urbaniczky C (1991) Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins. J Colloid Interface Sci 143:513–526
Bakrač B, Gutiérrez-Aguirre I, Podlesek Z, Sonnen AF-P, Gilbert RJC, Maček P et al (2008) Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin. J Biol Chem 283:18665–18677
Bakrač B, Kladnik A, Maček P, McHaffie G, Werner A, Lakey JH et al (2010) A toxin-based probe reveals cytoplasmic exposure of golgi sphingomyelin. J Biol Chem 285:22186–22195
Lenarčič T, Albert I, Böhm H, Hodnik V, Pirc K, Zavec AB et al (2017) Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins. Science 358:1431–1434
Mohri I, Taniike M, Okazaki I, Kagitani-Shimono K, Aritake K, Kanekiyo T et al (2006) Lipocalin-type prostaglandin D synthase is up-regulated in oligodendrocytes in lysosomal storage diseases and binds gangliosides: PGDS up-regulation in lysosomal storage disorders. J Neurochem 97:641–651
Li H, Zhao X, Wang J, Dong Y, Meng S, Li R et al (2016) β-sitosterol interacts with pneumolysin to prevent Streptococcus pneumoniae infection. Sci Rep 5:17668
Beseničar MP, Anderluh G (2010) Preparation of lipid membrane surfaces for molecular interaction studies by surface plasmon resonance biosensors. Methods Mol Biol 627:191–200
Cooper MA, Try AC, Carroll J, Ellar DJ, Williams DH (1998) Surface plasmon resonance analysis at a supported lipid monolayer. Biochim Biophys Acta 1373:101–111
Cooper MA, Hansson A, Löfås S, Williams DH (2000) A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors. Anal Biochem 277:196–205
Anderluh G, Beseničar M, Kladnik A, Lakey JH, Maček P (2005) Properties of nonfused liposomes immobilized on an L1 Biacore chip and their permeabilization by a eukaryotic pore-forming toxin. Anal Biochem 344:43–52
Bavdek A, Gekara NO, Priselac D, Gutiérrez Aguirre I, Darji A, Chakraborty T et al (2007) Sterol and pH interdependence in the binding, oligomerization, and pore formation of listeriolysin. Biochemistry 46:4425–4437
Myszka DG (1997) Kinetic analysis of macro molecular interactions using surface plasmon resonance biosensors. Anal Biotechnol 8:50–57
Stahelin RV, Cho W (2001) Differential roles of ionic, aliphatic, and aromatic residues in membrane–protein interactions: a surface plasmon resonance study on phospholipases A. Biochemistry 40:4672–4678
Kostan J, Salzer U, Orlova A, Törö I, Hodnik V, Senju Y et al (2014) Direct interaction of actin filaments with F-BAR protein pacsin 2. EMBO Rep 15:1154–1162
Shanmugham A, Wong Fong Sang HW, Bollen YJM, Lill H (2006) Membrane binding of twin arginine preproteins as an early step in translocation. Biochemistry 45:2243–2249
Bahloul A, Michel V, Hardelin J-P, Nouaille S, Hoos S, Houdusse A et al (2010) Cadherin-23, myosin VIIa and harmonin, encoded by Usher syndrome type I genes, form a ternary complex and interact with membrane phospholipids. Hum Mol Genet 19:3557–3565
Hekman M, Albert S, Galmiche A, Rennefahrt UEE, Fueller J, Fischer A et al (2006) Reversible membrane interaction of BAD requires two C-terminal lipid binding domains in conjunction with 14-3-3 protein binding. J Biol Chem 281:17321–17336
Locatelli-Hoops S, Remmel N, Klingenstein R, Breiden B, Rossocha M, Schoeniger M et al (2006) Saposin A mobilizes lipids from low cholesterol and high bis(monoacylglycerol)phosphate-containing membranes. J Biol Chem 281:32451–32460
Sugiki T, Takahashi H, Nagasu M, Hanada K, Shimada I (2010) Real-time assay method of lipid extraction activity. Anal Biochem 399:162–167
Beseničar MP, Bavdek A, Kladnik A, Maček P, Anderluh G (2008) Kinetics of cholesterol extraction from lipid membranes by methyl-β-cyclodextrin—a surface plasmon resonance approach. Biochim Biophys Acta 1778:175–184
Praper T, Beseničar MP, Istinič H, Podlesek Z, Metkar SS, Froelich CJ et al (2010) Human perforin permeabilizing activity, but not binding to lipid membranes, is affected by pH. Mol Immunol 47:2492–2504
Saenko E, Sarafanov A, Ananyeva N, Behre E, Shima M, Schwinn H et al (2001) Comparison of the properties of phospholipid surfaces formed on HPA and L1 biosensor chips for the binding of the coagulation factor VIII. J Chromatogr 921:49–56
Papo N, Shai Y (2003) Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. Biochemistry 42:458–466
Karlsson OP, Löfås S (2002) Flow-mediated on-surface reconstitution of G-protein coupled receptors for applications in surface plasmon resonance biosensors. Anal Biochem 300:132–138
Vidic JM, Grosclaude J, Persuy M-A, Aioun J, Salesse R, Pajot-Augy E (2006) Quantitative assessment of olfactory receptors activity in immobilized nanosomes: a novel concept for bioelectronic nose. Lab Chip 6:1026–1032
Brändén M, Tabaei SR, Fischer G, Neutze R, Höök F (2010) Refractive-index-based screening of membrane-protein-mediated transfer across biological membranes. Biophys J 99:124–133
Lundquist A, Hansen SB, Nordström H, Danielson UH, Edwards K (2010) Biotinylated lipid bilayer disks as model membranes for biosensor analyses. Anal Biochem 405:153–159
Hosseinkhani B, van den Akker N, D’Haen J, Gagliardi M, Struys T, Lambrichts I et al (2017) Direct detection of nano-scale extracellular vesicles derived from inflammation-triggered endothelial cells using surface plasmon resonance. Nanomedicine 13:1663–1671
Im H, Shao H, Park YI, Peterson VM, Castro CM, Weissleder R et al (2014) Label-free detection and molecular profiling of exosomes with a nano-plasmonic sensor. Nat Biotechnol 32(5):490–495
Zhu L, Wang K, Cui J, Liu H, Bu X, Ma H et al (2014) Label-free quantitative detection of tumor-derived exosomes through surface plasmon resonance imaging. Anal Chem 86:8857–8864
Grasso L, Wyss R, Weidenauer L, Thampi A, Demurtas D, Prudent M et al (2015) Molecular screening of cancer-derived exosomes by surface plasmon resonance spectroscopy. Anal Bioanal Chem 407:5425–5432
Rupert DLM, Lässer C, Eldh M, Block S, Zhdanov VP, Lotvall JO et al (2014) Determination of exosome concentration in solution using surface plasmon resonance spectroscopy. Anal Chem 86:5929–5936
Grover Shah V, Ray S, Karlsson R, Srivastava S (2015) Calibration-free concentration analysis of protein biomarkers in human serum using surface plasmon resonance. Talanta 144:801–808
Kobayashi M, Nishizawa M, Inoue N, Hosoya T, Yoshida M, Ukawa Y et al (2014) Epigallocatechin gallate decreases the micellar solubility of cholesterol via specific interaction with phosphatidylcholine. J Agric Food Chem 62:2881–2890
Zimmermann K, Eells R, Heinrich F, Rintoul S, Josey B, Shekhar P et al (2017) The cytosolic domain of T-cell receptor ζ associates with membranes in a dynamic equilibrium and deeply penetrates the bilayer. J Biol Chem 292:17746–17759
Hodnik V, Anderluh G (2010) Capture of intact liposomes on biacore sensor chips for protein–membrane interaction studies. Methods Mol Biol 627:201–211
Hall K, Aguilar MI (2010) Surface plasmon resonance spectroscopy for studying the membrane binding of antimicrobial peptides. Methods Mol Biol 627:213–223
Hodgkin MN, Masson MR, Powner D, Saqib KM, Ponting CP, Wakelam MJO (2000) Phospholipase D regulation and localisation is dependent upon a phosphatidylinositol 4,5-bisphosphate-specific PH domain. Curr Biol 10:43–46
Erb E-M, Chen X, Allen S, Roberts CJ, Tendler SJB, Davies MC et al (2000) Characterization of the surfaces generated by liposome binding to the modified dextran matrix of a surface plasmon resonance sensor chip. Anal Biochem 280:29–35
Marquês JT, de Almeida RFM, Viana AS (2014) Lipid bilayers supported on bare and modified gold – formation, characterization and relevance of lipid rafts. Electrochim Acta 126:139–150
Acknowledgments
We would like to thank the Slovenian Research Agency for the continuing support of the Infrastructural Centre for Molecular Interaction Analysis at the Department of Biology, Biotechnical Faculty, University of Ljubljana, Slovenia (program grant number I0-0022) and for the support of the program grant “Molecular interactions” (grant number P1-0391).
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Šakanovič, A., Hodnik, V., Anderluh, G. (2019). Surface Plasmon Resonance for Measuring Interactions of Proteins with Lipids and Lipid Membranes. 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_3
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DOI: https://doi.org/10.1007/978-1-4939-9512-7_3
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