Isothermal titration calorimetry (ITC): a standard operating procedure (SOP).
Calibration
Isothermal titration calorimetry
Ligand-binding equilibria
Standardization
Journal
European biophysics journal : EBJ
ISSN: 1432-1017
Titre abrégé: Eur Biophys J
Pays: Germany
ID NLM: 8409413
Informations de publication
Date de publication:
May 2021
May 2021
Historique:
received:
16
10
2020
accepted:
05
02
2021
revised:
05
11
2020
pubmed:
6
3
2021
medline:
30
11
2021
entrez:
5
3
2021
Statut:
ppublish
Résumé
Isothermal titration calorimetry (ITC) is currently widely used in many applied areas of research, spanning protein-ligand binding, metal-ligand interactions, DNA/DNA or protein/DNA interactions, partition to membranes, and polymer surfactant interactions, to mention just a few. This is due to the availability of commercial instruments, and thus the production and spread of an accepted and widely followed SOP is felt by most users, in an effort to produce results that are scientifically correct and comparable. Therefore, within the efforts of Working Group 4 of the ARBRE-MOBIEU COST Action (CA15126), this ITC SOP was generated, alongside SOPs for several other biophysical techniques. Here, we discuss the factors that are fundamental for good experimental design and that need to be carefully considered, as well as machine calibration, in particular chemical calibration, linked to another outcome of Working Group 4 on ITC benchmarking, to be also published in this Special Issue.
Identifiants
pubmed: 33665758
doi: 10.1007/s00249-021-01509-5
pii: 10.1007/s00249-021-01509-5
doi:
Substances chimiques
Ligands
0
Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
363-371Subventions
Organisme : Fundação para a Ciência e a Tecnologia
ID : UIDB/00081/2020
Organisme : Ministerio de Economía y Competitividad
ID : BFU2016-78232-P
Références
Bastos M (2016) Biocalorimetry: foundations and contemporary approaches, 1st Edition. CRC Press, Boca Raton. https://doi.org/10.1201/b20161
Bastos M, Briggner LE, Shehatta I, Wadso I (1990) The binding of alkane alpha-omega-diols to alpha-cyclodextrin—a microcalorimetric study. J ChemThermodyn 22:1181–1190. https://doi.org/10.1016/0021-9614(90)90111-3
doi: 10.1016/0021-9614(90)90111-3
Brautigam CA (2015) Fitting two- and three-site binding models to isothermal titration calorimetric data. Methods 76:124–136. https://doi.org/10.1016/j.ymeth.2014.11.018
doi: 10.1016/j.ymeth.2014.11.018
pubmed: 25484338
Brautigam CA, Zhao H, Vargas C, Keller S, Schuck P (2016) Integration and global analysis of isothermal titration calorimetry data for studying macromolecular interactions. Nat Protoc 11:882–894. https://doi.org/10.1038/nprot.2016.044
Broecker J, Vargas C, Keller S (2011) Revisiting the optimal c value for isothermal titration calorimetry. Anal Biochem 418:307–309. https://doi.org/10.1016/j.ab.2011.07.027
doi: 10.1016/j.ab.2011.07.027
pubmed: 21854755
Chaires JB (2008) Calorimetry and thermodynamics in drug design. Annu Rev Biophys 37:135–151. https://doi.org/10.1146/annurev.biophys.36.040306.132812
doi: 10.1146/annurev.biophys.36.040306.132812
pubmed: 18573076
Chaires JB, Hansen LD, Keller S, Brautigam CA, Zhao H, Schuck P (2015) Biocalorimetry. Methods 76:1–2. https://doi.org/10.1016/j.ymeth.2015.02.001
doi: 10.1016/j.ymeth.2015.02.001
pubmed: 25817327
Freire E, Schön A, Velazquez‐Campoy A (2009) Chapter 5 Isothermal titration calorimetry: general formalism using binding polynomials. In: Michael L, Johnson JMH, Gary KA (eds) Methods in enzymology, vol 455. Academic Press, pp 127–155. https://doi.org/10.1016/S0076-6879(08)04205-5
Garbett NC, Chaires JB (2008) Binding: a polemic and rough guide. Methods Cell Biol 84:3–23. https://doi.org/10.1016/S0091-679X(07)84001-5
doi: 10.1016/S0091-679X(07)84001-5
pubmed: 17964926
Hansen LD, Fellingham GW, Russell DJ (2011) Simultaneous determination of equilibrium constants and enthalpy changes by titration calorimetry: methods, instruments, and uncertainties. Anal Biochem 409:220–229. https://doi.org/10.1016/j.ab.2010.11.002
doi: 10.1016/j.ab.2010.11.002
pubmed: 21073852
Jarmoskaite I, Al-Sadhan I, Vaidyanathan PP, Herschlag D (2020) How to measure and evaluate binding affinities. eLife 9:e57264. https://doi.org/10.7554/eLife.57264
doi: 10.7554/eLife.57264
pubmed: 32758356
pmcid: 7452723
Kantonen SA, Henriksen NM, Gilson MK (2017) Evaluation and minimization of uncertainty in ITC binding measurements: heat error, concentration error, saturation, and stoichiometry. BiochimBiophysActa Gen Subj 1861:485–498. https://doi.org/10.1016/j.bbagen.2016.09.002
doi: 10.1016/j.bbagen.2016.09.002
Krainer G, Keller S (2014) Single-experiment displacement assay for quantifying high-affinity binding by isothermal titration calorimetry. Methods. https://doi.org/10.1016/j.ymeth.2014.10.034
doi: 10.1016/j.ymeth.2014.10.034
pubmed: 25461813
Krainer G, Broecker J, Vargas C, Fanghänel J, Keller S (2012) Quantifying high-affinity binding of hydrophobic ligands by isothermal titration calorimetry. Anal Chem 84:10715–10722
doi: 10.1021/ac3025575
Markova N, Hallén D (2004) The development of a continuous isothermal titration calorimetric method for equilibrium studies. Anal Biochem 331:77–88
doi: 10.1016/S0003-2697(04)00254-4
Piñeiro Á et al (2019) AFFINImeter: a software to analyze molecular recognition processes from experimental data. Anal Biochem 577:117–134. https://doi.org/10.1016/j.ab.2019.02.031
doi: 10.1016/j.ab.2019.02.031
pubmed: 30849378
Privalov PL (2012) Microcalorimetry of macrocomolecules. Wiley, Amsterdam
doi: 10.1002/9781118337509
Regina A, Guangyue YB, Watson L, Bastos M (2012) Chemical calibration of isothermal titration calorimeters: an evaluation of the dilution of propan-1-ol into water as a test reaction using different calorimeters, concentrations, and temperatures. J ChemThermodyn 52:57–63. https://doi.org/10.1016/j.jct.2011.12.018
doi: 10.1016/j.jct.2011.12.018
Schon A, Lam SY, Freire E (2011a) Thermodynamics-based drug design: strategies for inhibiting protein-protein interactions. Future Med Chem 3:1129–1137. https://doi.org/10.4155/fmc.11.81
doi: 10.4155/fmc.11.81
pubmed: 21806377
pmcid: 3164996
Schon A, Madani N, Smith AB, Lalonde JM, Freire E (2011b) Some binding-related drug properties are dependent on thermodynamic signature. ChemBiol Drug Des 77:161–165. https://doi.org/10.1111/j.1747-0285.2010.01075.x
doi: 10.1111/j.1747-0285.2010.01075.x
Tellinghuisen J (2005) Simple algorithms for nonlinear calibration by the classical and standard additions methods. Analyst 130:370–378. https://doi.org/10.1039/b411054d
doi: 10.1039/b411054d
pubmed: 15724167
Tellinghuisen J (2007) Calibration in isothermal titration calorimetry: heat and cell volume from heat of dilution of NaCl(aq). Anal Biochem 360:47–55. https://doi.org/10.1016/j.ab.2006.10.015
doi: 10.1016/j.ab.2006.10.015
pubmed: 17107650
Tellinghuisen J (2008) Isothermal titration calorimetry at very low c. Anal Biochem 373:395–397. https://doi.org/10.1016/j.ab.2007.08.039
doi: 10.1016/j.ab.2007.08.039
pubmed: 17920027
Tellinghuisen J (2009) Least squares in calibration: weights, nonlinearity, and other nuisances. Methods Enzymol 454:259–285. https://doi.org/10.1016/S0076-6879(08)03810-X
doi: 10.1016/S0076-6879(08)03810-X
pubmed: 19216930
Tellinghuisen J (2012) Designing isothermal titration calorimetry experiments for the study of 1:1 binding: problems with the “standard protocol.” Anal Biochem 424:211–220. https://doi.org/10.1016/j.ab.2011.12.035
doi: 10.1016/j.ab.2011.12.035
pubmed: 22306472
Tellinghuisen J (2016a) Optimizing isothermal titration calorimetry protocols for the study of 1:1 binding: keeping it simple. BiochimBiophysActa 1860:861–867. https://doi.org/10.1016/j.bbagen.2015.10.011
doi: 10.1016/j.bbagen.2015.10.011
Tellinghuisen J (2016b) Analysis of multitemperature isothermal titration calorimetry data at very low c: Global beats van’t Hoff. Anal Biochem 513:43–46. https://doi.org/10.1016/j.ab.2016.08.024
doi: 10.1016/j.ab.2016.08.024
pubmed: 27567993
Tellinghuisen J (2018) Critique of methods for estimating heats in isothermal titration calorimetry. Anal Biochem 563:79–86. https://doi.org/10.1016/j.ab.2018.08.015
doi: 10.1016/j.ab.2018.08.015
pubmed: 30149027
Tellinghuisen J (2019) Calibration: detection, quantification, and confidence limits are (almost) exact when the data variance function is known. Anal Chem 91:8715–8722. https://doi.org/10.1021/acs.analchem.9b00119
doi: 10.1021/acs.analchem.9b00119
pubmed: 31180654
Vega S, Abian O, Velazquez-Campoy A (2015) A unified framework based on the binding polynomial for characterizing biological systems by isothermal titration calorimetry. Methods 76:99–115. https://doi.org/10.1016/j.ymeth.2014.09.010
doi: 10.1016/j.ymeth.2014.09.010
pubmed: 25305413
Vega S, Abian O, Velazquez-Campoy A (2019) Handling complexity in biological interactions. J Therm Anal Calorim 138:3229–3248. https://doi.org/10.1007/s10973-019-08610-0
doi: 10.1007/s10973-019-08610-0
Velazquez-Campoy A (2015) Geometric features of the Wiseman isotherm in isothermal titration calorimetry. J Therm Anal Calorim 122:1477–1483. https://doi.org/10.1007/s10973-015-4775-x
doi: 10.1007/s10973-015-4775-x
Velazquez-Campoy A, Freire E (2005) ITC in the post-genomic era...? Priceless BiophysChem 115:115–124. https://doi.org/10.1016/j.bpc.2004.12.015
doi: 10.1016/j.bpc.2004.12.015
Velazquez-Campoy A, Freire E (2006) Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nat Protoc 1:186–191
doi: 10.1038/nprot.2006.28
Velazquez-Campoy A, Ohtaka H, Nezami A, Muzammil S, Freire E (2004) Isothermal titration calorimetry. In: Bonifacino BS et al (eds) Curr Protocol Cell Biology/editorial board, Chapter 17:Unit 17 18 https://doi.org/10.1002/0471143030.cb1708s23
Zhao H, Piszczek G, Schuck P (2015) SEDPHAT—a platform for global ITC analysis and global multi-method analysis of molecular interactions. Methods (San Diego, Calif) 76:137–148. https://doi.org/10.1016/j.ymeth.2014.11.012
doi: 10.1016/j.ymeth.2014.11.012