Abstract
Isothermal titration calorimetry (ITC) is a well-established technique that allows the accurate and precise determination of binding equilibrium constants. It is able to provide detailed thermodynamic description of reacting systems without the need for van’t Hoff analysis. ITC plays an important role in biology, biochemistry and medicinal chemistry, providing researchers with important information on the structure, stability and functionality of biological and synthetic molecules. This review demonstrates the power and versatility of ITC in providing accurate, rapid, and label-free measurement of the thermodynamics of molecular interactions. Moreover, this work focuses on recent studies employing ITC to investigate compounds of great biotechnological interest.
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References
Berman, H.M., et al.: The protein data bank. Nucleic Acids Res. 28(1), 235–242 (2000)
Christensen, J.J., Johnston, H.D., Izatt, R.M.: An isothermal titration calorimeter. Rev. Sci. Instrum. 39(9), 1356–1359 (1968)
Wiseman, T., et al.: Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179(1), 131–137 (1989)
Horn, J.R., Brandts, J.F., Murphy, K.P.: van’t Hoff and calorimetric enthalpies II: effects of linked equilibria. Biochemistry 41(23), 7501–7507 (2002)
Horn, J.R., et al.: van’t Hoff and calorimetric enthalpies from isothermal titration calorimetry: are there significant discrepancies? Biochemistry 40(6), 1774–1778 (2001)
Kantonen, S.A., Henriksen, N.M., Gilson, M.K.: Accounting for apparent deviations between calorimetric and van’t Hoff enthalpies. Biochim. Biophys. Acta 1862, 692–704 (2018)
Liu, Y., Sturtevant, J.M.: Significant discrepancies between van’t Hoff and calorimetric enthalpies. II. Protein Sci. 4(12), 2559–2561 (1995)
Liu, Y., Sturtevant, J.M.: Significant discrepancies between van’t Hoff and calorimetric enthalpies. III. Biophys. Chem. 64(1–3), 121–126 (1997)
Naghibi, H., Tamura, A., Sturtevant, J.M.: Significant discrepancies between van’t Hoff and calorimetric enthalpies. Proc. Natl. Acad. Sci. U.S.A. 92(12), 5597–5599 (1995)
Turnbull, W.B., Daranas, A.H.: On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc. 125(48), 14859–14866 (2003)
Velazquez-Campoy, A., Freire, E.: Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nat. Protoc. 1(1), 186–191 (2006)
Khalifah, R.G., et al.: Thermodynamics of binding of the carbon dioxide-competitive inhibitor imidazole and related compounds to human carbonic anhydrase I: an isothermal titration calorimetry approach to studying weak binding by displacement with strong inhibitors. Biochemistry 32(12), 3058–3066 (1993)
Zhang, Y.L., Zhang, Z.Y.: Low-affinity binding determined by titration calorimetry using a high-affinity coupling ligand: a thermodynamic study of ligand binding to protein tyrosine phosphatase 1B. Anal. Biochem. 261(2), 139–148 (1998)
Sigurskjold, B.W.: Exact analysis of competition ligand binding by displacement isothermal titration calorimetry. Anal. Biochem. 277(2), 260–266 (2000)
Tellinghuisen, J.: Designing isothermal titration calorimetry experiments for the study of 1:1 binding: problems with the “standard protocol”. Anal. Biochem. 424(2), 211–220 (2012)
Nilsson, S.O., Wadso, I.: A flow-microcalorimetric vessel for solution of small quantities of easily or slightly soluble liquids—solution of benzene in water at 298.15-K. J. Chem. Thermodyn. 16(4), 317–330 (1984)
Mizoue, L.S., Tellinghuisen, J.: The role of backlash in the “first injection anomaly” in isothermal titration calorimetry. Anal. Biochem. 326(1), 125–127 (2004)
Markova, N., Hallen, D.: The development of a continuous isothermal titration calorimetric method for equilibrium studies. Anal. Biochem. 331(1), 77–88 (2004)
Christensen, J.J., Hansen, L.D., Izatt, R.M.: Handbook of Proton Ionization Heats and Related Thermodynamic Quantities. Wiley, New York (1976)
Goldberg, R.N., Kishore, N., Lennen, R.M.: Thermodynamic quantities for the ionization reactions of buffers. J. Phys. Chem. Ref. Data 31(2), 231–370 (2002)
de Rivera, M.R., Socorro, F.: Baseline changes in an isothermal titration microcalorimeter. J. Therm. Anal. Calorim. 80(3), 769–773 (2005)
Bhatnagar, R.S., Gordon, J.I.: Thermodynamic studies of myristoyl-coa—protein N-myristoyltransferase using isothermal titration calorimetry. Lipid Modif. Proteins 250, 467–486 (1995)
Brautigam, C.A.: Fitting two- and three-site binding models to isothermal titration calorimetric data. Methods 76, 124–136 (2015)
Brown, A.: Analysis of cooperativity by isothermal titration calorimetry. Int. J. Mol. Sci. 10(8), 3457–3477 (2009)
McPhail, D., Cooper, A.: Thermodynamics and kinetics of dissociation of ligand-induced dimers of vancomycin antibiotics. J. Chem. Soc. Faraday Trans. 93(13), 2283–2289 (1997)
Buurma, N.J., Haq, I.: Advances in the analysis of isothermal titration calorimetry data for ligand-DNA interactions. Methods 42(2), 162–172 (2007)
Keeler, C., et al.: An explicit formulation approach for the analysis of calcium binding to EF-hand proteins using isothermal titration calorimetry. Biophys. J. 105(12), 2843–2853 (2013)
Freire, E., Schon, A., Velazquez-Campoy, A.: Isothermal titration calorimetry: general formalism using binding polynomials. Methods Enzymol. 455, 127–155 (2009)
Ladbury, J.E.: Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design. Biochem. Soc. Trans. 38(4), 888–893 (2010)
Fisher, H.F., Singh, N.: Calorimetric methods for interpreting protein-ligand interactions. Energ. Biol. Macromol. 259, 194–221 (1995)
Ladbury, J.E., Chowdhry, B.Z.: Sensing the heat: the application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions. Chem. Biol. 3(10), 791–801 (1996)
Livingstone, J.R., Spolar, R.S., Record Jr., M.T.: Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry 30(17), 4237–4244 (1991)
Spolar, R.S., Livingstone, J.R., Record, M.T.: Use of liquid-hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry 31(16), 3947–3955 (1992)
Sturtevant, J.M.: Heat capacity and entropy changes in processes involving proteins. Proc. Natl. Acad. Sci. U.S.A 74(6), 2236–2240 (1977)
Gomez, J., Freire, E.: Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. 252(3), 337–350 (1995)
Haq, I., et al.: Specific binding of hoechst 33258 to the d(CGCAAATTTGCG)2 duplex: calorimetric and spectroscopic studies. J. Mol. Biol. 271(2), 244–257 (1997)
Chaires, J.B.: Energetics of drug-DNA interactions. Biopolymers 44(3), 201–215 (1997)
Cooper, A.: Thermodynamic analysis of biomolecular interactions. Curr. Opin. Chem. Biol. 3(5), 557–563 (1999)
Holdgate, G.A., Ward, W.H.: Measurements of binding thermodynamics in drug discovery. Drug Discov. Today 10(22), 1543–1550 (2005)
Spolar, R.S., Record Jr., M.T.: Coupling of local folding to site-specific binding of proteins to DNA. Science 263(5148), 777–784 (1994)
Jeffrey, G.A., Saenger, W.: Hydrogen Bonding in Biological Structures. Springer, New York (1991)
Fersht, A.: Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding, vol. xxi, 631 p. W.H. Freeman, New York (1999)
Scatena, L.F., Brown, M.G., Richmond, G.L.: Water at hydrophobic surfaces: weak hydrogen bonding and strong orientation effects. Science 292(5518), 908–912 (2001)
Matulis, D.: Thermodynamics of the hydrophobic effect. III. Condensation and aggregation of alkanes, alcohols, and alkylamines. Biophys. Chem. 93(1), 67–82 (2001)
Matulis, D., Bloomfield, V.A.: Thermodynamics of the hydrophobic effect. II. Calorimetric measurement of enthalpy, entropy, and heat capacity of aggregation of alkylamines and long aliphatic chains. Biophys. Chem. 93(1), 53–65 (2001)
Matulis, D., Bloomfield, V.A.: Thermodynamics of the hydrophobic effect. I. Coupling of aggregation and pK(a) shifts in solutions of aliphatic amines. Biophys. Chem. 93(1), 37–51 (2001)
Matulis, D., Rouzina, I., Bloomfield, V.A.: Thermodynamics of DNA binding and condensation: isothermal titration calorimetry and electrostatic mechanism. J. Mol. Biol. 296(4), 1053–1063 (2000)
Ahmad, M., et al.: Enthalpy-entropy compensation upon molecular conformational changes. J. Chem. Theory Comput. 11(4), 1410–1418 (2015)
Breiten, B., et al.: Water networks contribute to enthalpy/entropy compensation in protein-ligand binding. J. Am. Chem. Soc. 135(41), 15579–15584 (2013)
Dragan, A.I., Read, C.M., Crane-Robinson, C.: Enthalpy-entropy compensation: the role of solvation. Eur. Biophys. J. 46(4), 301–308 (2017)
Dunitz, J.D.: Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2(11), 709–712 (1995)
Lee, B.: Enthalpy-entropy compensation in the thermodynamics of hydrophobicity. Biophys. Chem. 51(2–3), 271–277; discussion 277–278 (1994)
Holdgate, G.A.: Making cool drugs hot: isothermal titration calorimetry as a tool to study binding energetics. Biotechniques 31(1), 164–166, 168, 170 passim (2001)
Baldwin, R.L.: Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. U.S.A. 83(21), 8069–8072 (1986)
Privalov, P.L., Gill, S.J.: Stability of protein structure and hydrophobic interaction. Adv. Protein Chem. 39, 191–234 (1988)
Spolar, R.S., Ha, J.H., Record Jr., M.T.: Hydrophobic effect in protein folding and other noncovalent processes involving proteins. Proc. Natl. Acad. Sci. U.S.A. 86(21), 8382–8385 (1989)
Kelley, R.F., O’Connell, M.P.: Thermodynamic analysis of an antibody functional epitope. Biochemistry 32(27), 6828–6835 (1993)
Davies, T.G., Hubbard, R.E., Tame, J.R.: Relating structure to thermodynamics: the crystal structures and binding affinity of eight OppA-peptide complexes. Protein Sci. 8(7), 1432–1444 (1999)
Chaires, J.B.: Calorimetry and thermodynamics in drug design. Ann. Rev. Biophys. 37, 135–151 (2008)
Garbett, N.C., Chaires, J.B.: Thermodynamic studies for drug design and screening. Expert Opin. Drug Discov. 7(4), 299–314 (2012)
Pierce, M.M., Raman, C.S., Nall, B.T.: Isothermal titration calorimetry of protein-protein interactions. Methods 19(2), 213–221 (1999)
Freire, E., Mayorga, O.L., Straume, M.: Isothermal titration calorimetry. Anal. Chem. 62(18), A950–A959 (1990)
Lewis, E.A., Murphy, K.P.: Isothermal titration calorimetry. Methods Mol. Biol. 305, 1–16 (2005)
Leavitt, S., Freire, E.: Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr. Opin. Struct. Biol. 11(5), 560–566 (2001)
Ababou, A., Ladbury, J.E.: Survey of the year 2004: literature on applications of isothermal titration calorimetry. J. Mol. Recognit. 19(1), 79–89 (2006)
Cliff, M.J., Ladbury, J.E.: A survey of the year 2002 literature on applications of isothermal titration calorimetry. J. Mol. Recogn. 16(6), 383–391 (2003)
Ghai, R., Falconer, R.J., Collins, B.M.: Applications of isothermal titration calorimetry in pure and applied research–survey of the literature from 2010. J. Mol. Recogn. 25(1), 32–52 (2012)
Falconer, R.J.: Applications of isothermal titration calorimetry—the research and technical developments from 2011 to 2015. J. Mol. Recogn. 29(10), 504–515 (2016)
Majhi, P.R., Blume, A.: Thermodynamic characterization of temperature-induced micellization and demicellization of detergents studied by differential scanning calorimetry. Langmuir 17(13), 3844–3851 (2001)
Vargas, C., Klingler, J., Keller, S.: Membrane partitioning and translocation studied by isothermal titration calorimetry. Methods Mol. Biol. 1033, 253–271 (2013)
Poncet-Legrand, C., et al.: Interactions between flavan-3-ols and poly(L-proline) studied by isothermal titration calorimetry: effect of the tannin structure. J. Agric. Food Chem. 55(22), 9235–9240 (2007)
Zheng, Y., et al.: Effect of pH on the complexation of kaempferol-4′-glucoside with three beta-cyclodextrin derivatives: isothermal titration calorimetry and spectroscopy study. J. Agric. Food Chem. 62(1), 244–250 (2014)
Baldoni, D., et al.: Performance of microcalorimetry for early detection of methicillin resistance in clinical isolates of Staphylococcus aureus. J. Clin. Microbiol. 47(3), 774–776 (2009)
Xi, L., et al.: Microcalorimetric study of Staphylococcus aureus growth affected by selenium compounds. Thermochim. Acta 387(1), 57–61 (2002)
Mariana, F., et al.: Isothermal titration calorimetry—a new method for the quantification of microbial degradation of trace pollutants. J. Microbiol. Methods 82(1), 42–48 (2010)
Hansen, L.D., et al.: Enzyme-catalyzed and binding reaction kinetics determined by titration calorimetry. Biochim. Biophys. Acta 1860(5), 957–966 (2016)
Transtrum, M.K., Hansen, L.D., Quinn, C.: Enzyme kinetics determined by single-injection isothermal titration calorimetry. Methods 76, 194–200 (2015)
Demarse, N.A., et al.: Determining enzyme kinetics via isothermal titration calorimetry. Methods Mol. Biol. 978, 21–30 (2013)
Todd, M.J., Gomez, J.: Enzyme kinetics determined using calorimetry: a general assay for enzyme activity? Anal. Biochem. 296(2), 179–187 (2001)
Hughes, J.P., et al.: Principles of early drug discovery. Br. J. Pharmacol. 162(6), 1239–1249 (2011)
Ruben, A.J., Kiso, Y., Freire, E.: Overcoming roadblocks in lead optimization: a thermodynamic perspective. Chem. Biol. Drug Des. 67(1), 2–4 (2006)
Torres, F.E., et al.: Higher throughput calorimetry: opportunities, approaches and challenges. Curr. Opin. Struct. Biol. 20(5), 598–605 (2010)
Zhou, X., Kini, R.M., Sivaraman, J.: Application of isothermal titration calorimetry and column chromatography for identification of biomolecular targets. Nat. Protoc. 6(2), 158–165 (2011)
Malmsten, M.: Soft drug delivery systems. Soft Matter 2(9), 760–769 (2006)
Gwinn, M.R., Vallyathan, V.: Nanoparticles: health effects—pros and cons. Environ. Health Perspect. 114(12), 1818–1825 (2006)
Cedervall, T., et al.: Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. Angew. Chem. Int. Ed. Engl. 46(30), 5754–5756 (2007)
Saptarshi, S.R., Duschl, A., Lopata, A.L.: Interaction of nanoparticles with proteins: relation to bio-reactivity of the nanoparticle. J. Nanobiotechnol. 11, 26 (2013)
Mandal, S., et al.: Interaction of carbon nanoparticles to serum albumin: elucidation of the extent of perturbation of serum albumin conformations and thermodynamical parameters. J. Hazard. Mater. 248–249, 238–245 (2013)
Malmsten, M.: Inorganic nanomaterials as delivery systems for proteins, peptides, DNA, and siRNA. Curr. Opin. Colloid Interface Sci. 18(5), 468–480 (2013)
Cukalevski, R., et al.: Structural changes in apolipoproteins bound to nanoparticles. Langmuir 27(23), 14360–14369 (2011)
Cedervall, T., et al.: Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc. Natl. Acad. Sci. 104(7), 2050–2055 (2007)
Fleischer, C.C., Payne, C.K.: Secondary structure of corona proteins determines the cell surface receptors used by nanoparticles. J. Phys. Chem. B 118(49), 14017–14026 (2014)
Eren, N.M., Narsimhan, G., Campanella, O.H.: Protein adsorption induced bridging flocculation: the dominant entropic pathway for nano-bio complexation. Nanoscale 8(6), 3326–3336 (2016)
Decher, G., Schlenoff, J.B.: Multilayer thin Films: Sequential Assembly Of Nanocomposite Materials. 2nd compl. rev. and enl. edn. Wiley, Weinheim (2012)
Dan, N.: The structure of DNA complexes with cationic liposomes-cylindrical or flat bilayers? Biochim. Biophys. Acta 1369(1), 34–38 (1998)
Golan, R., et al.: DNA toroids: stages in condensation. Biochemistry 38(42), 14069–14076 (1999)
Vilfan, I.D., et al.: Time study of DNA condensate morphology: implications regarding the nucleation, growth, and equilibrium populations of toroids and rods. Biochemistry 45(26), 8174–8183 (2006)
Perspicace, S., et al.: Isothermal titration calorimetry with micelles: Thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein. FEBS Open Bio 3, 204–211 (2013)
Loh, W., Brinatti, C., Tam, K.C.: Use of isothermal titration calorimetry to study surfactant aggregation in colloidal systems. Biochim. Biophys. Acta 1860(5), 999–1016 (2016)
Marsh, D.: Thermodynamics of phospholipid self-assembly. Biophys. J. 102(5), 1079–1087 (2012)
Feng, X., Leduc, M., Pelton, R.: Polyelectrolyte complex characterization with isothermal titration calorimetry and colloid titration. Colloids Surf. A 317(1), 535–542 (2008)
Maurstad, G., Kitamura, S., Stokke, B.T.: Isothermal titration calorimetry study of the polyelectrolyte complexation of xanthan and chitosan samples of different degree of polymerization. Biopolymers 97(1), 1–10 (2012)
Lounis, F.M., et al.: Interactions between oppositely charged polyelectrolytes by isothermal titration calorimetry: effect of ionic strength and charge density. J. Phys. Chem. B 121(12), 2684–2694 (2017)
Manning, G.S.: Limiting laws and counterion condensation in polyelectrolyte solutions I. Colligative properties. J. Chem. Phys. 51(3), 924–933 (1969)
Sideratou, Z., et al.: Arginine end-functionalized poly(L-lysine) dendrigrafts for the stabilization and controlled release of insulin. J. Colloid Interface Sci. 351(2), 433–441 (2010)
Bulbake, U., et al.: Liposomal formulations in clinical use: an updated review. Pharmaceutics 9(2), 12 (2017)
Sercombe, L., et al.: Advances and challenges of liposome assisted drug delivery. Front Pharmacol 6, 286 (2015)
Ikonen, M., Murtomaki, L., Kontturi, K.: Microcalorimetric and zeta potential study on binding of drugs on liposomes. Colloids Surf B Biointerfaces 78(2), 275–282 (2010)
Al-Kaddah, S., et al.: Analysis of membrane interactions of antibiotic peptides using ITC and biosensor measurements. Biophys. Chem. 152(1), 145–152 (2010)
Allain, V., Bourgaux, C., Couvreur, P.: Self-assembled nucleolipids: from supramolecular structure to soft nucleic acid and drug delivery devices. Nucleic Acids Res. 40(5), 1891–1903 (2012)
Thanassoulas, A., et al.: From nucleobases to nucleolipids: an ITC approach on the thermodynamics of their interactions in aqueous solutions. J. Phys. Chem. B 118(24), 6570–6585 (2014)
Patwa, A., et al.: Tuning molecular interactions in lipid-oligonucleotides assemblies via locked nucleic acid (LNA)-based lipids. Org. Biomol. Chem. 11(41), 7108–7112 (2013)
Lipinski, C.A.: Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods 44(1), 235–249 (2000)
Amidon, G.L., et al.: A theoretical basis for a biopharmaceutic drug classification: the correlation of in vitro drug product dissolution and in vivo bioavailability. Pharm. Res. 12(3), 413–420 (1995)
Gidwani, B., Vyas, A.: A comprehensive review on cyclodextrin-based carriers for delivery of chemotherapeutic cytotoxic anticancer drugs. Biomed. Res. Int. 2015, 198268 (2015)
Villiers, A.: Sur la fermentation de la fécule par l’action du ferment butyrique. Compt. Rend. Acad. Sci 112, 536–538 (1891)
Lipinski, C.A., et al.: Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46(1–3), 3–26 (2001)
Marttin, E., Verhoef, J.C., Merkus, F.W.: Efficacy, safety and mechanism of cyclodextrins as absorption enhancers in nasal delivery of peptide and protein drugs. J. Drug Target. 6(1), 17–36 (1998)
Connors, K.A.: The stability of cyclodextrin complexes in solution. Chem. Rev. 97(5), 1325–1358 (1997)
Segura-Sanchez, F., et al.: Elucidation of the complexation mechanism between (+)-usnic acid and cyclodextrins studied by isothermal titration calorimetry and phase-solubility diagram experiments. J. Mol. Recogn. 22(3), 232–241 (2009)
Mazzaferro, S., et al.: Bivalent sequential binding of docetaxel to methyl-beta-cyclodextrin. Int. J. Pharm. 416(1), 171–180 (2011)
Ignaczak, A., Palecz, B., Belica-Pacha, S.: Quantum chemical study and isothermal titration calorimetry of beta-cyclodextrin complexes with mianserin in aqueous solution. Org. Biomol. Chem. 15(5), 1209–1216 (2017)
Agnes, M., et al.: Designed positively charged cyclodextrin hosts with enhanced binding of penicillins as carriers for the delivery of antibiotics: the case of oxacillin. Int. J. Pharm. 531(2), 480–491 (2017)
Nguyen, H.H., et al.: Surface plasmon resonance: a versatile technique for biosensor applications. Sens. (Basel) 15(5), 10481–10510 (2015)
Piliarik, M., Vaisocherova, H., Homola, J.: Surface plasmon resonance biosensing. Methods Mol. Biol. 503, 65–88 (2009)
Tyszka, J.M., Fraser, S.E., Jacobs, R.E.: Magnetic resonance microscopy: recent advances and applications. Curr. Opin. Biotechnol. 16(1), 93–99 (2005)
Cala, O., Guilliere, F., Krimm, I.: NMR-based analysis of protein-ligand interactions. Anal. Bioanal. Chem. 406(4), 943–956 (2014)
Lebowitz, J., Lewis, M.S., Schuck, P.: Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 11(9), 2067–2079 (2002)
Howlett, G.J., Minton, A.P., Rivas, G.: Analytical ultracentrifugation for the study of protein association and assembly. Curr. Opin. Chem. Biol. 10(5), 430–436 (2006)
Rossi, A.M., Taylor, C.W.: Analysis of protein-ligand interactions by fluorescence polarization. Nat. Protoc. 6(3), 365–387 (2011)
Hall, M.D., et al.: Fluorescence polarization assays in high-throughput screening and drug discovery: a review. Methods Appl. Fluoresci. 4(2), 022001 (2016)
Heegaard, N.H., Nilsson, S., Guzman, N.A.: Affinity capillary electrophoresis: important application areas and some recent developments. J. Chromatogr. B Biomed. Sci. Appl. 715(1), 29–54 (1998)
Albishri, H.M., et al.: Recent advances in affinity capillary electrophoresis for binding studies. Bioanalysis 6(24), 3369–3392 (2014)
Hofstadler, S.A., Sannes-Lowery, K.A.: Applications of ESI-MS in drug discovery: interrogation of noncovalent complexes. Nat. Rev. Drug Discov. 5(7), 585–595 (2006)
Vivat Hannah, V., et al.: Native MS: an ‘ESI’ way to support structure- and fragment-based drug discovery. Future Med. Chem. 2(1), 35–50 (2010)
Freyer, M.W., Lewis, E.A.: Isothermal titration calorimetry: experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions. Methods Cell Biol. 84, 79–113 (2008)
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Thanassoulas, A., Nounesis, G. (2019). Isothermal Titration Calorimetry: A Powerful Tool for the Characterization of Molecular Interactions. In: Demetzos, C., Pippa, N. (eds) Thermodynamics and Biophysics of Biomedical Nanosystems. Series in BioEngineering. Springer, Singapore. https://doi.org/10.1007/978-981-13-0989-2_4
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