Membrane-induced conformational change in human apolipoprotein H

Shao Xiong Wang, Yu Tong Sun, Sen Fang Sui

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

The interaction of apolipoprotein H (Apo H) with lipid membrane has been considered to be a basic mechanism for the biological function of the protein. Previous reports have demonstrated that Apo H can interact only with membranes containing anionic phospholipids. Here we study the membrane-induced conformational change of Apo H by CD spectroscopy with two different model systems: anionic-phospholipid-containing liposomes [such as 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) and cardiolipin], and the water/methanol mixtures at moderately low pH, which mimic the micro-physicochemical environment near the membrane surface. It is found that Apo H undergoes a remarkable conformational change on interaction with liposomes containing anionic phospholipid. To interact with liposomes containing DMPG, there is a 6.8% increase in α-helix in the secondary structures; in liposomes containing cardiolipin, however, there is a 12.6% increase in α-helix and a 9% decrease in β-sheet. The similar conformation change in Apo H can be induced by treatment with an appropriate mixture of water/methanol. The results indicate that the association of Apo H with membrane is correlated with a certain conformational change in the secondary structure of the protein.

Original languageEnglish (US)
Pages (from-to)103-106
Number of pages4
JournalBiochemical Journal
Volume348
Issue number1
DOIs
StatePublished - May 15 2000
Externally publishedYes

Keywords

  • Circular dichroism
  • Lipid-protein interaction
  • Protein adsorption
  • β-glycoprotein I

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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