Isothermal titration calorimetry for characterization of recombinant proteins

Current Opinion in Biotechnology
Lina BaranauskienėDaumantas Matulis

Abstract

Isothermal titration calorimetry is widely used to measure the affinities and enthalpies of interaction between proteins and/or small molecules. The quantitative nature of the technique is especially useful in the characterization of recombinant proteins while determining the fraction of protein capable of binding a specific ligand and thus the protein purity. The revealed thermodynamic information sheds light on the binding mechanism, important for the targeted drug design of the biologics. Here we show examples how, together with the thermal shift assay, combination of both techniques enables characterization of protein stability and ligand binding. Furthermore, the binding-linked reactions that strongly affect the observed thermodynamic parameters and must be dissected to obtain the intrinsic parameters that are necessary for the structure-based rational drug design are being demonstrated using inhibitors of Hsp90, an anticancer target protein.

Citations

May 31, 2019·Expert Opinion on Drug Discovery·Visvaldas KairysEgidijus Kazlauskas
Dec 5, 2020·International Journal of Biological Macromolecules·Sefli Sri Wahyu EffendiI-Son Ng
Apr 19, 2021·Allergy·Maksymilian ChruszczHeimo Breiteneder
Jul 13, 2021·Frontiers in Pharmacology·Santhosh BabyStephen Lewis
Jul 16, 2021·International Journal of Biological Macromolecules·Aisha Fahim, Onofrio Annunziata
Oct 29, 2021·Biotechnology and Bioengineering·Makiko HorikawaMasahiro Kawahara

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