Conformational changes of beta-lactoglobulin induced by anionic phospholipid.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Liu, X; Shang, L; Jiang, X; Dong, S; Wang, E

Published Date

  • June 1, 2006

Published In

Volume / Issue

  • 121 / 3

Start / End Page

  • 218 - 223

PubMed ID

  • 16494994

Pubmed Central ID

  • 16494994

International Standard Serial Number (ISSN)

  • 0301-4622

Digital Object Identifier (DOI)

  • 10.1016/j.bpc.2005.12.015

Language

  • eng

Conference Location

  • Netherlands