Conformational changes of β-lactoglobulin induced by anionic phospholipid

Xiaohua Liu; Li Shang; Xiue Jiang; Shaojun Dong; Erkang Wang

doi:10.1016/j.bpc.2005.12.015

Conformational changes of β-lactoglobulin induced by anionic phospholipid

Xiaohua Liu, Li Shang, Xiue Jiang, Shaojun Dong, Erkang Wang

Research output: Contribution to journal › Article › peer-review

49 Scopus citations

Abstract

Conformational changes of β-lactoglobulin (β-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 β-LG-DMPG interactions cause β-LG a structural reorganization of the secondary structure elements accompanied by an increase in α-helical content, and a loosening of the protein tertiary structure. The interaction forces between β-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.

Original language	English
Pages (from-to)	218-223
Number of pages	6
Journal	Biophysical Chemistry
Volume	121
Issue number	3
DOIs	https://doi.org/10.1016/j.bpc.2005.12.015
State	Published - 1 Jun 2006
Externally published	Yes

Keywords

β-lactoglobulin
Circular dichroism
Conformational changes
DMPG
Fluorescence
UV-VIS

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10.1016/j.bpc.2005.12.015

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title = "Conformational changes of β-lactoglobulin induced by anionic phospholipid",

abstract = "Conformational changes of β-lactoglobulin (β-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 β-LG-DMPG interactions cause β-LG a structural reorganization of the secondary structure elements accompanied by an increase in α-helical content, and a loosening of the protein tertiary structure. The interaction forces between β-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.",

keywords = "β-lactoglobulin, Circular dichroism, Conformational changes, DMPG, Fluorescence, UV-VIS",

author = "Xiaohua Liu and Li Shang and Xiue Jiang and Shaojun Dong and Erkang Wang",

year = "2006",

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doi = "10.1016/j.bpc.2005.12.015",

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TY - JOUR

T1 - Conformational changes of β-lactoglobulin induced by anionic phospholipid

AU - Liu, Xiaohua

AU - Shang, Li

AU - Jiang, Xiue

AU - Dong, Shaojun

AU - Wang, Erkang

PY - 2006/6/1

Y1 - 2006/6/1

N2 - Conformational changes of β-lactoglobulin (β-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 β-LG-DMPG interactions cause β-LG a structural reorganization of the secondary structure elements accompanied by an increase in α-helical content, and a loosening of the protein tertiary structure. The interaction forces between β-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.

AB - Conformational changes of β-lactoglobulin (β-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 β-LG-DMPG interactions cause β-LG a structural reorganization of the secondary structure elements accompanied by an increase in α-helical content, and a loosening of the protein tertiary structure. The interaction forces between β-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.

KW - β-lactoglobulin

KW - Circular dichroism

KW - Conformational changes

KW - DMPG

KW - Fluorescence

KW - UV-VIS

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DO - 10.1016/j.bpc.2005.12.015

M3 - 文章

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SN - 0301-4622

VL - 121

SP - 218

EP - 223

JO - Biophysical Chemistry

JF - Biophysical Chemistry

IS - 3

ER -

Conformational changes of β-lactoglobulin induced by anionic phospholipid

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Keywords

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