Denaturation of Lysozyme Using a Porphyrin Derivative Bearing Multiple Anionic Groups
Tetraphenylporphyrin derivatives bearing multifunctional groups in the side chains are found to be excellent receptors interacting with protein exteriors for various proteins. In the present study, the recognition and denaturation of lysozyme using tetracarboxyphenylporphyrin was studied using circular dichroism (CD) spectroscopy. The absorption in the far UV CD spectrum (around 230 nm) attributed to the secondary structure of lysozyme was decreased by adding the porphyrin. The pH and ionic strength in aqueous solution was found to influence the denaturation by the porphyrin.Under optimal conditions, lysozyme is efficiently denatured only in the presence of a two molar equivalent of the porphyrin compound. The stoichiometry of the complexation between lysozyme and the porphyrin was investigated from a quantitative analysis of the denaturation using CD spectra. The Job plot and slope analysis for the amount of denatured protein confirmed that they form a 1 : 1 complex. These results indicate that the anionic porphyrin receptor acts as an efficient denaturant for lysozyme.
denaturation protein surface recognition porphyrin lysozyme circular dichroism
TATSUYA OSHIMA HIROSHI MUTO KAORU OHE YOSHINARI BABA
Department of Applied Chemistry, Faculty of Engineering, University of Miyazaki, 1-1, Gakuen Kibanadai Nishi, Miyazaki, 889-2192, Japan
国际会议
The 12th Asian Pacific Confederation of Chemical Engineering Congress(第十二届亚太化工联盟大会暨化工展览会)
大连
英文
2008-08-04（万方平台首次上网日期，不代表论文的发表时间）