Isothermal microcalorimetry to investigate non specific interactions in biophysical chemistry.

International Journal of Molecular Sciences
Vincent Ball, Clarisse Maechling

Abstract

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.

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Methods Mentioned

BETA
X-ray
NMR
isothermal titration microcalorimetry
electrophoresis
isothermal titration
differential scanning calorimetry
small
angle neutron scattering
transfection

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