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Study on the Interaction between Lanthanide Cationic Porphyrin Complex and Bovine Serum Albumin
Author(s) -
Liu Peng,
Liu Yi,
Li Xi,
Huang WeiGuo
Publication year - 2007
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.200790178
Subject(s) - chemistry , porphyrin , cationic polymerization , bovine serum albumin , quenching (fluorescence) , lanthanide , photochemistry , enthalpy , absorption spectroscopy , förster resonance energy transfer , fluorescence , absorption (acoustics) , polymer chemistry , organic chemistry , chromatography , thermodynamics , ion , physics , quantum mechanics , acoustics
The interaction between lanthanide cationic porphyrin and bovine serum albumin (BSA) was studied by fluorescence and UV‐Vis spectrum. The static quenching of BSA was observed in the presence of YbTMPyP. According to the thermodynamic parameters, this binding was regarded as "enthalpy‐driven" reaction. Furthermore, YbTMPyP is so close to the residues of BSA that molecular resonance energy transfer occurs between them. Besides, the red drift and hypochromicity of absorption spectrum of YbTMPyP were accompanied with the binding reaction.