Conformational changes of beta-lactoglobulin induced by anionic phospholipid |
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Authors: | Liu Xiaohua Shang Li Jiang Xiue Dong Shaojun Wang Erkang |
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Affiliation: | State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Renmin Street 5625, Changchun, Jilin 130022, China. |
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Abstract: | Conformational changes of beta-lactoglobulin (beta-LG) induced by anionic phospholipid (dimyristoylphosphatidylglycerol, DMPG) at physiological conditions (pH 7.0) have been investigated by UV-VIS, circular dichroism (CD) and fluorescence spectra. The experimental results suggest that beta-LG-DMPG interactions cause beta-LG a structural reorganization of the secondary structure elements accompanied by an increase in alpha-helical content, and a loosening of the protein tertiary structure. The interaction forces between beta-LG and DMPG are further evaluated by fluorescence spectra. The fluorescence spectral data show that conformational changes in the protein are driven by electrostatic interaction at first, then by hydrophobic interaction between a protein with a negative net charge and a negatively charged phospholipid. |
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Keywords: | β-lactoglobulin DMPG Conformational changes UV–VIS Circular dichroism Fluorescence |
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