| 光谱学与光谱分析 |
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| Studies on the Spectral Characteristics of Efficient HIV-1 Fusion Inhibitor C22 |
| SHI Jun1,2,HE Jiao-juan1,WANG Shi-long1*,SUN Xiao-yu1,CHEN Qing-yu2 |
1.School of Life Science and Technology, Tongji University, Shanghai 200092, China
2.Anhui Science and Technical University, Bengbu 233100, China |
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Abstract Acquired immune deficiency syndrome (AIDS) is increasing its negative influences on human society and economy.In the present paper, HIV-1 cell fusion peptide inhibitor C22 was expressed and purified based on the C-terminal sequence of HIV-l membrane fusion glycoprotein gp41.The gene coding for C22 was totally synthesized using gp41 gene as a template and amplified by PCR.The cloned C22 gene was confirmed by restriction endonuclease and sequence analysis and then cloned into plasmid pTMHa30-51.The prepared plasmid was transformed into E.coli BL21 (DE3) and the expressing products were analyzed on SDS-PAGE and tested with mass spectrum.The results indicated that C22 showed high HIV-1 fusion inhibiting capacity, meanwhile, with good thermal stability and water-solubility, and showed no cell toxicity in tested concentrations.The spectral characteristics were tested with circular dichroism (CD).When treated at different temperature in solution condition, the content of α helix of C22 increased at 37 ℃ while decreased sharply at 80 ℃.The peak value changed significantly with different pH values.The content of α helix of C22 decreased as pH varied toward acid and alkali and the random coiling increased, which led to a relaxed structure.This result indicated that the C22 structure is stable with pH 6.This research may provide a theoretic foundation for the new type HIV-1 peptide inhibitor designing and spectral characteristics study.
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Received: 2007-08-28
Accepted: 2007-11-28
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Corresponding Authors:
WANG Shi-long
E-mail: wsl@mail.tongji.edu.cn
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