THERMODYNAMIC CHARACTERIZATION OF METAL PHTHALOCYANINES-HUMAN SERUM ALBUMIN INTERACTIONS.

The temperature dependence of the binding constants for human serum albumin and sulfonated metal-phthalocyanines were estimated by fluorescence spectroscopy. Stern-Volmer's analysis and Chipman's fits provided binding data for van't Hoff calculations of the thermodynamic parameters governing these interactions. Results show that the formations of the HSA- phthalocyanine complexes are favorable processes by both the ΔH° and ΔS°. However, the formation of HSA-AIPcS4 has a stronger dependence than HSA-ZnPcS 4on ΔS°.