Isothermal titration calorimetry for characterization of recombinant proteins

Lina Baranauskiene, Tai Chih Kuo, Wen Yih Chen, Daumantas Matulis

研究成果: 雜誌貢獻回顧型文獻

1 引文 (Scopus)

摘要

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.
原文英語
頁(從 - 到)9-15
頁數7
期刊Current Opinion in Biotechnology
55
DOIs
出版狀態已發佈 - 二月 1 2019

指紋

Recombinant proteins
Calorimetry
Titration
Recombinant Proteins
Drug Design
Proteins
Thermodynamics
Ligands
Protein Stability
Biological Products
Protein Binding
Hot Temperature
Pharmaceutical Preparations
Enthalpy
Assays
Molecules

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering

引用此文

Isothermal titration calorimetry for characterization of recombinant proteins. / Baranauskiene, Lina; Kuo, Tai Chih; Chen, Wen Yih; Matulis, Daumantas.

於: Current Opinion in Biotechnology, 卷 55, 01.02.2019, p. 9-15.

研究成果: 雜誌貢獻回顧型文獻

Baranauskiene, Lina ; Kuo, Tai Chih ; Chen, Wen Yih ; Matulis, Daumantas. / Isothermal titration calorimetry for characterization of recombinant proteins. 於: Current Opinion in Biotechnology. 2019 ; 卷 55. 頁 9-15.
@article{ab982329057d433698c192248555c8ed,
title = "Isothermal titration calorimetry for characterization of recombinant proteins",
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.",
author = "Lina Baranauskiene and Kuo, {Tai Chih} and Chen, {Wen Yih} and Daumantas Matulis",
year = "2019",
month = "2",
day = "1",
doi = "10.1016/j.copbio.2018.06.003",
language = "English",
volume = "55",
pages = "9--15",
journal = "Current Opinion in Biotechnology",
issn = "0958-1669",
publisher = "Elsevier Limited",

}

TY - JOUR

T1 - Isothermal titration calorimetry for characterization of recombinant proteins

AU - Baranauskiene, Lina

AU - Kuo, Tai Chih

AU - Chen, Wen Yih

AU - Matulis, Daumantas

PY - 2019/2/1

Y1 - 2019/2/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85049986813&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85049986813&partnerID=8YFLogxK

U2 - 10.1016/j.copbio.2018.06.003

DO - 10.1016/j.copbio.2018.06.003

M3 - Review article

VL - 55

SP - 9

EP - 15

JO - Current Opinion in Biotechnology

JF - Current Opinion in Biotechnology

SN - 0958-1669

ER -