Isothermal Microcalorimetry to Investigate Non Specific Interactions in Biophysical Chemistry

International Journal of Molecular Sciences

Vincent Ball¹ 

[1] Institut National de la Santé et de la Recherche Médicale, Unité mixte de recherche 977, 11 rue Humann, 67085 Strasbourg Cédex, France

关键词: non-specific interactions;    isothermal titration calorimetry;   

DOI  :  10.3390/ijms10083283

来源: mdpi

【 摘 要 】

Isothermal titration microcalorimetry (ITC) is mostly used to investigate the thermodynamics of “specific” host-guest interactions in biology as well as in supramolecular chemistry. The aim of this review is to demonstrate that ITC can also provide useful information about non-specific interactions, like electrostatic or hydrophobic interactions. More attention will be given in the use of ITC to investigate polyelectrolyte-polyelectrolyte (in particular DNA-polycation), polyelectrolyte-protein as well as protein-lipid interactions. We will emphasize that in most cases these “non specific” interactions, as their definition will indicate, are favoured or even driven by an increase in the entropy of the system. The origin of this entropy increase will be discussed for some particular systems. We will also show that in many cases entropy-enthalpy compensation phenomena occur.

【 授权许可】

CC BY   
© 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.