Acta Phys. -Chim. Sin. ›› 2011, Vol. 27 ›› Issue (08): 1907-1912.doi: 10.3866/PKU.WHXB20110822

• SOFT MATTER • Previous Articles     Next Articles

Structural Property of Hemoglobin in Span 80/PEG 400/H2O Niosome System

WANG Yuan-You1,2, HUA Wei1, LIU Tian-Qing1   

  1. 1. School of Chemistry and Chemical Engineering, Yangzhou University, Yangzhou 225002, Jiangsu Province, P. R. China;
    2. Department of Chemical Engineering, Yangzhou Polytechnic Institute, Yangzhou 225127, Jiangsu Province, P. R. China
  • Received:2011-02-28 Revised:2011-05-18 Published:2011-07-19
  • Contact: LIU Tian-Qing E-mail:tqliu@yzu.edu.cn
  • Supported by:

    The project was supported by the National Natural Science Foundation of China (20573091).

Abstract:

The structural property of hemoglobin (Hb) was studied in detail by UV-Vis absorption, fluorescence, circular dichroism, negative staining-transmission electron microscopy (NS-TEM), and freeze etching-transmission electron microscopy (FE-TEM) techniques using a Span 80/PEG 400/H2O niosome system. The obtained results show that Hb is adsorbed onto the surface of niosome. The peptide chain of Hb spreads out and the apparent radius of the niosome, the intensities of the UV-Vis absorption peaks, and the fluorescence peaks increase. For the second structural parameter of Hb, the α-helix content decreases but the β-sheet and β-turn content increases. The stability of Hb varies with that of the niosome.

Key words: Hemoglobin, Structure, Property, Niosome

MSC2000: 

  • O648