Study on the interaction between lanthanide cationic porphyrin complex and bovine serum albumin

Peng Liu*, Yi Liu, Xi Li, Wei Guo Huang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)917-920
Number of pages4
JournalChinese Journal of Chemistry
Volume25
Issue number7
DOIs
Publication statusPublished - Jul 2007

Scopus Subject Areas

  • Chemistry(all)

User-Defined Keywords

  • BSA
  • Enthalpy-driven
  • Fluorescence
  • Hypochromicity
  • Porphyrin

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