ITC in the post-genomic era...? Priceless

Adrián Velazquez-Campoy, Ernesto Freire

Research output: Contribution to journalArticlepeer-review

Abstract

The information available after decoding the genome of the human species and many others is opening the possibility of new approaches to target thousands of protein interactions critical for a continuously increasing list of genetic and infectious diseases and pathologies, and to understand complex regulatory pathways and interaction networks describing cell function and interrelation. There is a need for a reliable technique offering the capability of measuring accurately macromolecular interactions (e.g. protein/ligand, protein/protein, protein/nucleic acid) in the laboratory. Compared to other analytical techniques, isothermal titration calorimetry (ITC) exhibits some important advantages for characterizing intermolecular interactions and binding equilibria. ITC is suitable for characterizing both low affinity interactions (e.g. protein network regulation and natural ligands) and high affinity interactions (e.g. rational drug design). Considering the advanced technological level reached as well as the outstanding quality of the information accessible through this technique, ITC is expected to play a very prominent role in the next years in the areas of rational drug design and protein network regulation.

Original languageEnglish (US)
Pages (from-to)115-124
Number of pages10
JournalBiophysical Chemistry
Volume115
Issue number2-3 SPEC. ISS.
DOIs
StatePublished - Apr 1 2005

Keywords

  • Binding equilibrium
  • Extreme binding affinity
  • Isothermal titration calorimetry
  • Thermodynamics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry

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