Thermodynamic study of the imipramine–insulin interaction
✍ Scribed by José Luis López-Fontán; Victor Mosquera; Carlos Rega; Félix Sarmiento; Malcom N. Jones
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 169 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0021-9614
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✦ Synopsis
The interaction of the antidepressant drug imipramine with insulin in aqueous solution at pH = 3.2 (ionic strength I c = 6.5•10 -3 mol • dm -3 ) has been investigated by equilibrium dialysis and microcalorimetry. Imipramine binds to insulin to the extent of ≈(50 to 60) imipramine molecules per insulin molecule in the temperature range T = (283.15 to 308.15) K. The binding data have been used to obtain the Gibbs energy per imipramine molecule bound G ν using the Wyman binding potential approach. The enthalpy of the interaction is small and exothermic following a sigmoidal curve as a function of binding, and G ν is dominated by a large entropy increase on binding which is of similar magnitude to the non-specific hydrophobic binding of several other amphipathic ligands with globular proteins.
📜 SIMILAR VOLUMES
## Abstract Thermal decomposition of imipramine hydrochloride and trimipramine maleate has been investigated isothermally and nonisothermally. The kinetic parameters, namely the activation energy __E__~a~ and the Arrhenius preexponential term __A__, were calculated. Applying the theory of activated