Chem. J. Chinese Universities ›› 2009, Vol. 30 ›› Issue (8): 1509.

• Articles • Previous Articles     Next Articles

Spectroscopic Studies on the Interaction of Murexide and Murexide-Copper Complex with Human Serum Albumin

MA Ping1, CHI Yan-Hua1*, ZHUANG Jia2, WANG Han1, CHEN Liang1, LIU Xu1, DONG Fa-Qin1   

  1. 1. Department of Chemistry, School of Materials Science and Engineering, Southwest University of Science and Technology, Mianyang 621010, China;
    2. School of Materials Science and Engineering, Southwest Petroleum University, Chengdu 610500, China
  • Received:2008-07-14 Online:2009-08-10 Published:2009-08-10
  • Contact: CHI Yan-Hua
  • Supported by:

    国家自然科学基金(批准号: 20271042, 10776027)和电分析化学国家重点实验室基金(批准号: 2008007)资助.

Abstract:

The interactions of human serum albumin(HSA) with murexide(Mx) and murexide-copper complex(Mx-Cu2+) were investigated by fluorescence spectroscopy and Fourier transform infrared spectroscopy(FTIR) under simulative physiological conditions. The results show Mx and Mx-Cu2+ could quench the intrinsic fluorescence of HSA by static quenching and hydrophobic interaction was the predominant intermolecular force. The binding constant of Mx and HSA was increased in the presence of copper(Ⅱ). According to fluorescence resonance energy transfer(FRET), the distancer between donor(HSA) and acceptor(Mx and Mx-Cu2+) were calculated to be 2.82 and 2.53 nm, the ternary system energy transfer efficiency E′> binary system E, which showed the copper ion acts as the energy transfer agency. The synchronous fluorescence and FTIR study suggested that Mx and Mx-Cu2+ can cause almost the same changes in the secondary structure of HSA. Upon binding with Mx or Mx-Cu2+ complex, the α-helix structure was reduced more than 8%, the β-sheet reduced 1%, while the β-turn increased 6%, and the random coil increased 4%. The results show that the main factor of secondary structure changing is Mx.

Key words: Murexide and murexide-copper complex; Human serum albumin; Fluorescence spectroscopy; Fourier transform infrared spectroscopy; Secondary structure

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