Penetration of human apolipoprotein H into air/water interface with and without phospholipid monolayers

Yutong Sun, Shao Xiong Wang, Sen Fang Sui

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Apolipoprotein H (β2-glycoprotein I) is a 54 kDa plasma glycoprotein. The interaction of ApoH with phospholipids has been demonstrated to be involved in the regulation of the function of the activated platelets and the clearance of phosphotidylserine (PS)-expressing cells. In the present work, the monolayer technique is employed to characterize the feature of the penetration of ApoH into air/water interface with and without phospholipid monolayers. The results indicate that ApoH can penetrate into the air/water interface and there is a protein-concentration dependent lag time in the adsorption isotherm. ApoH can insert into the phospholipid monolayers spread at the air/water interface, but no lag time is observed in this case. The fact that ApoH prefers to interact with anionic phospholipid monolayers suggests that the negative charges of the phospholipid monolayers may play an important role in the process of the membrane insertion of ApoH.

Original languageEnglish (US)
Pages (from-to)105-112
Number of pages8
JournalColloids and Surfaces A: Physicochemical and Engineering Aspects
Volume175
Issue number1-2
DOIs
StatePublished - Dec 15 2000

Fingerprint

beta 2-Glycoprotein I
Phospholipids
Monolayers
penetration
Hydrogen
Water
air
time lag
Air
Glycoproteins
water
clearances
inserts
platelets
insertion
isotherms
membranes
proteins
Beam plasma interactions
Platelets

Keywords

  • Apolipoprotein II
  • Membrane insertion
  • Phospholipid monolayers

ASJC Scopus subject areas

  • Surfaces and Interfaces
  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Penetration of human apolipoprotein H into air/water interface with and without phospholipid monolayers. / Sun, Yutong; Wang, Shao Xiong; Sui, Sen Fang.

In: Colloids and Surfaces A: Physicochemical and Engineering Aspects, Vol. 175, No. 1-2, 15.12.2000, p. 105-112.

Research output: Contribution to journalArticle

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N2 - Apolipoprotein H (β2-glycoprotein I) is a 54 kDa plasma glycoprotein. The interaction of ApoH with phospholipids has been demonstrated to be involved in the regulation of the function of the activated platelets and the clearance of phosphotidylserine (PS)-expressing cells. In the present work, the monolayer technique is employed to characterize the feature of the penetration of ApoH into air/water interface with and without phospholipid monolayers. The results indicate that ApoH can penetrate into the air/water interface and there is a protein-concentration dependent lag time in the adsorption isotherm. ApoH can insert into the phospholipid monolayers spread at the air/water interface, but no lag time is observed in this case. The fact that ApoH prefers to interact with anionic phospholipid monolayers suggests that the negative charges of the phospholipid monolayers may play an important role in the process of the membrane insertion of ApoH.

AB - Apolipoprotein H (β2-glycoprotein I) is a 54 kDa plasma glycoprotein. The interaction of ApoH with phospholipids has been demonstrated to be involved in the regulation of the function of the activated platelets and the clearance of phosphotidylserine (PS)-expressing cells. In the present work, the monolayer technique is employed to characterize the feature of the penetration of ApoH into air/water interface with and without phospholipid monolayers. The results indicate that ApoH can penetrate into the air/water interface and there is a protein-concentration dependent lag time in the adsorption isotherm. ApoH can insert into the phospholipid monolayers spread at the air/water interface, but no lag time is observed in this case. The fact that ApoH prefers to interact with anionic phospholipid monolayers suggests that the negative charges of the phospholipid monolayers may play an important role in the process of the membrane insertion of ApoH.

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