Isothermal microcalorimetry to investigate non specific interactions in biophysical chemistry.
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.
Ball
Vincent
V
Institut National de la Santé et de la Recherche Médicale, Unité mixte de recherche 977, 11 rue Humann, 67085 Strasbourg Cédex, France.|Université de Strasbourg, Faculté de Chirurgie Dentaire, 1 Place de l'Hôpital, 67000 Strasbourg, France.
Maechling
Clarisse
C
Laboratoire d'Innovation Thérapeutique, Unité Mixte de Recherche 7200 CNRS - Université de Strasbourg, Faculté de Pharmacie, 74 route du Rhin BP 60024, F-67401 ILLKIRCH Cedex, France.
D002151:Calorimetry; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004573:Electrolytes / Q000737:chemistry; D007700:Kinetics; D011073:Polyamines / Q000737:chemistry*; D000071228:Polyelectrolytes; D013816:Thermodynamics
D004247:DNA; D004573:Electrolytes; D011073:Polyamines; D000071228:Polyelectrolytes