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Thermodynamic Analysis of the Interaction between Cationic Porphyrins and Human Serum Albumin by an Optical Biosensor
Author(s) -
YiMin Qin,
NiNa Pan,
YongXing Jian,
ZaoYing Li,
GuoLin Zou
Publication year - 2005
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200591095
Subject(s) - chemistry , biosensor , cuvette , enthalpy , cationic polymerization , human serum albumin , gibbs free energy , fluorescence , bovine serum albumin , fluorescence spectroscopy , analytical chemistry (journal) , thermodynamics , chromatography , organic chemistry , biochemistry , physics , quantum mechanics
An optical biosensor with a stirred cuvette has been used to monitor the interaction between immobilized human serum albumin (HSA) and three water‐soluble cationic porphyrins. The binding constants at 25 °C obtained from biosensor analysis were compared with those from fluorescence spectroscopy. The interactions were further investigated at temperatures from 15 °C to 30 °C. The thermodynamics parameters, changes of free energy (Δ G ), enthalpy (Δ H ) and entropy (Δ S ), were evaluated from equilibrium data. It appeared that the binding process was governed primarily by electrostatic forces.