Isothermal titration calorimetry in the single-injection mode with imperfect mixing.
ITC
Multiple-injection method
Single-injection method
Titration curve equations
Journal
European biophysics journal : EBJ
ISSN: 1432-1017
Titre abrégé: Eur Biophys J
Pays: Germany
ID NLM: 8409413
Informations de publication
Date de publication:
Jan 2022
Jan 2022
Historique:
received:
01
10
2020
accepted:
24
12
2021
revised:
19
12
2021
pubmed:
10
1
2022
medline:
12
2
2022
entrez:
9
1
2022
Statut:
ppublish
Résumé
Isothermal titration calorimetry (ITC) is now a method of choice to obtain thermodynamic information about the interaction between two molecular partners. Most often, the method in use is the so-called multiple-injection method (MIM) consisting in distinct short-time injections of the titrant separated by sufficient delay to reach equilibrium before each new injection. However, an alternative single-injection method (SIM) exists. It consists in a unique continuous injection and, despite the fact that it is quite simple and generally faster than MIM, it is very little used. The goal of this work is to reconsider its theoretical basis. A new equation taking into account the effect of dilution resulting from the continuous titration process is obtained. It allows to consider efficiently the continuum of possibilities from perfect to imperfect mixing of the cell content. It is shown that, to good approximation, imperfect mixing can be accounted for by considering the cell volume as an adjustable parameter. Most likely, this should lead to an artificial increase of it, although one cannot reject the possibility of a decrease. The processing of experimental data on the interaction of Ba
Identifiants
pubmed: 34999938
doi: 10.1007/s00249-021-01588-4
pii: 10.1007/s00249-021-01588-4
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
77-84Informations de copyright
© 2022. European Biophysical Societies' Association.
Références
Bianconi ML (2007) Calorimetry of enzyme-catalyzed reactions. Biophys Chem 126:59–64. https://doi.org/10.1016/j.bpc.2006.05.017
doi: 10.1016/j.bpc.2006.05.017
pubmed: 16824668
Briggner L-E, Wadsö I (1991) Test and calibration processes for microcalorimeters, with special reference to heat conduction instruments used with aqueous systems. J Biochem Biophys Methods 22:101–118. https://doi.org/10.1016/0165-022x(91)90023-p
doi: 10.1016/0165-022x(91)90023-p
pubmed: 2061558
Burnouf D, Ennifar E, Guedich S et al (2012) kinITC: a new method for obtaining joint thermodynamic and kinetic data by isothermal titration calorimetry. J Am Chem Soc 134:559–565. https://doi.org/10.1021/ja209057d
doi: 10.1021/ja209057d
pubmed: 22126339
Calvet E (1962) Experimental thermochemistry. In: Skinner HA (ed) Interscience. Springer, New York, pp 385–410
Chaires JB, Hansen LD, Keller S et al (2015) Biocalorimetry. Methods (san Diego, Calif) 76:1–2
doi: 10.1016/j.ymeth.2015.02.001
Dumas P (2016) Joining thermodynamics and kinetics by kinITC. In: Bastos M (ed) CRC Press, Boca Raton, pp 281–300
Dumas P (2019) Preprint withdrawn: not to be cited anymore. Rigorous equations for isothermal titration calorimetry: theoretical and practical consequences. Biorxiv. https://doi.org/10.1101/512780
doi: 10.1101/512780
Dumas P, Ennifar E, Da Veiga C et al (2016) Extending ITC to kinetics with kinITC. Methods Enzymol 567:157–180. https://doi.org/10.1016/bs.mie.2015.08.026
doi: 10.1016/bs.mie.2015.08.026
pubmed: 26794354
Eigen M, De Maeyer L (1963) Techniques of organic chemistry. Wiley, New York
Garrido PF, Bastos M, Velázquez-Campoy A et al (2022) Unsupervised bubble calorimetry analysis: surface tension from isothermal titration calorimetry. J Colloid Interface Sci 606:1823–1832. https://doi.org/10.1016/j.jcis.2021.08.115
doi: 10.1016/j.jcis.2021.08.115
pubmed: 34507173
Hansen CW, Hansen LD, Nicholson AD et al (2010) Correction for instrument time constant and baseline in determination of reaction kinetics. Int J Chem Kinet 43:53–61. https://doi.org/10.1002/kin.20530
doi: 10.1002/kin.20530
Herrera I, Winnik MA (2013) Differential binding models for isothermal titration calorimetry: moving beyond the Wiseman isotherm. J Phys Chem B 117:8659–8672
doi: 10.1021/jp311812a
Izatt RM, Bradshaw JS, Nielsen SA et al (1985) Thermodynamic and kinetic data for cation-macrocycle interaction. Chem Rev 85:271–339. https://doi.org/10.1021/cr00068a003
doi: 10.1021/cr00068a003
Markova N, Hallen D (2004) The development of a continuous isothermal titration calorimetric method for equilibrium studies. Anal Biochem 331:77–88. https://doi.org/10.1016/s0003-2697(04)00254-4
doi: 10.1016/s0003-2697(04)00254-4
pubmed: 15245999
Piñeiro Á, Muñoz E, Sabín J et al (2019) AFFINImeter: a software to analyze molecular recognition processes from experimental data. Anal Biochem. https://doi.org/10.1016/j.ab.2019.02.031
doi: 10.1016/j.ab.2019.02.031
pubmed: 30849378
Poon GMK (2010) Explicit formulation of titration models for isothermal titration calorimetry. Anal Biochem 400:229–236. https://doi.org/10.1016/j.ab.2010.01.025
doi: 10.1016/j.ab.2010.01.025
pubmed: 20100451
Sigurskjold BW (2000) Exact analysis of competition ligand binding by displacement isothermal titration calorimetry. Anal Biochem 277:260–266
doi: 10.1006/abio.1999.4402
Tellinghuisen J (2007a) Optimizing experimental parameters in isothermal titration calorimetry: variable volume procedures. J Phys Chem B 111:11531–11537. https://doi.org/10.1021/jp074515p
doi: 10.1021/jp074515p
pubmed: 17850136
Tellinghuisen J (2007b) 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 (2004) Volume errors in isothermal titration calorimetry. Anal Biochem 333:405–406. https://doi.org/10.1016/j.ab.2004.05.061
doi: 10.1016/j.ab.2004.05.061
pubmed: 15450820
Transtrum MK, Hansen LD, Quinn C (2015) Enzyme kinetics determined by single-injection isothermal titration calorimetry. Methods 76:194–200. https://doi.org/10.1016/j.ymeth.2014.12.003
doi: 10.1016/j.ymeth.2014.12.003
pubmed: 25497059
Vander-Meulen KA, Butcher SE (2011) Characterization of the kinetic and thermodynamic landscape of RNA folding using a novel application of isothermal titration calorimetry. Nucleic Acids Res 40:2140–2151. https://doi.org/10.1093/nar/gkr894
doi: 10.1093/nar/gkr894
pubmed: 22058128
pmcid: 3300012
Wiseman T, Williston S, Brandts JF, Lin LN (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179:131–137
doi: 10.1016/0003-2697(89)90213-3