Conformational changes of beta-lactoglobulin induced by anionic phospholipid.
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.
Liu
Xiaohua
X
State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Renmin Street 5625, Changchun, Jilin 130022, China.
Shang
Li
L
Jiang
Xiue
X
Dong
Shaojun
S
Wang
Erkang
E
D000838:Anions; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins / Q000737:chemistry*; D008958:Models, Molecular; D010715:Phosphatidylglycerols / Q000737:chemistry*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry
D000838:Anions; D007782:Lactoglobulins; D010715:Phosphatidylglycerols; C002773:dimyristoylphosphatidylglycerol