Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic α-helices

Matthew A. Mitsche, Donald M. Small

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Amphipathic α-helices (AαH) are the primary structural motif of exchangeable apolipoproteins. AαHs in exchangeable apolipoproteins adsorb, remodel, and desorb at the surface of plasma lipoproteins in response to changes in their size or composition. A triolein/water (TO/W) interface was used as a model surface to study adsorption and desorption of AαHs at a lipoprotein-like interface. We previously reported that AαH peptides spontaneously adsorb to a TO/W interface, but they only partially desorb from the surface when the excess peptide was removed from the system. This finding suggests that "exchangeable" apolipoproteins are in fact partially exchangeable and only desorb from a surface in response to compression or change in composition. Here, we develop a thermodynamic and kinetic model to describe this phenomenon based on the change in the interfacial pressure (Π) of the C-terminal 46 amino acids of apolipoprotein A-I (C46) at a TO/W interface. This model suggests that apolipoproteins have at least two interfacial conformations that are in a surface concentration and Π-dependent equilibrium. This two-state surface equilibrium model, which is based on experimental data and is consistent with dynamic changes in Π(t), provides insights into the selective metabolism and clearance of plasma lipoproteins and the process of lipoprotein remodeling.

Original languageEnglish (US)
Pages (from-to)1578-1588
Number of pages11
JournalJournal of Lipid Research
Volume54
Issue number6
DOIs
StatePublished - Jun 1 2013

Fingerprint

Apolipoproteins
Triolein
Lipoproteins
Conformations
Pressure
Water
Peptides
Apolipoprotein A-I
Plasmas
Thermodynamics
Adsorption
Surface states
Chemical analysis
Metabolism
Desorption
Amino Acids
Kinetics

Keywords

  • Apolipoproteins
  • Lipoprotein remodeling
  • Protein-lipid interactions

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Endocrinology

Cite this

Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic α-helices. / Mitsche, Matthew A.; Small, Donald M.

In: Journal of Lipid Research, Vol. 54, No. 6, 01.06.2013, p. 1578-1588.

Research output: Contribution to journalArticle

@article{334baadb7e884fc3b7616ffc20179673,
title = "Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic α-helices",
abstract = "Amphipathic α-helices (AαH) are the primary structural motif of exchangeable apolipoproteins. AαHs in exchangeable apolipoproteins adsorb, remodel, and desorb at the surface of plasma lipoproteins in response to changes in their size or composition. A triolein/water (TO/W) interface was used as a model surface to study adsorption and desorption of AαHs at a lipoprotein-like interface. We previously reported that AαH peptides spontaneously adsorb to a TO/W interface, but they only partially desorb from the surface when the excess peptide was removed from the system. This finding suggests that {"}exchangeable{"} apolipoproteins are in fact partially exchangeable and only desorb from a surface in response to compression or change in composition. Here, we develop a thermodynamic and kinetic model to describe this phenomenon based on the change in the interfacial pressure (Π) of the C-terminal 46 amino acids of apolipoprotein A-I (C46) at a TO/W interface. This model suggests that apolipoproteins have at least two interfacial conformations that are in a surface concentration and Π-dependent equilibrium. This two-state surface equilibrium model, which is based on experimental data and is consistent with dynamic changes in Π(t), provides insights into the selective metabolism and clearance of plasma lipoproteins and the process of lipoprotein remodeling.",
keywords = "Apolipoproteins, Lipoprotein remodeling, Protein-lipid interactions",
author = "Mitsche, {Matthew A.} and Small, {Donald M.}",
year = "2013",
month = "6",
day = "1",
doi = "10.1194/jlr.M034462",
language = "English (US)",
volume = "54",
pages = "1578--1588",
journal = "Journal of Lipid Research",
issn = "0022-2275",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "6",

}

TY - JOUR

T1 - Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic α-helices

AU - Mitsche, Matthew A.

AU - Small, Donald M.

PY - 2013/6/1

Y1 - 2013/6/1

N2 - Amphipathic α-helices (AαH) are the primary structural motif of exchangeable apolipoproteins. AαHs in exchangeable apolipoproteins adsorb, remodel, and desorb at the surface of plasma lipoproteins in response to changes in their size or composition. A triolein/water (TO/W) interface was used as a model surface to study adsorption and desorption of AαHs at a lipoprotein-like interface. We previously reported that AαH peptides spontaneously adsorb to a TO/W interface, but they only partially desorb from the surface when the excess peptide was removed from the system. This finding suggests that "exchangeable" apolipoproteins are in fact partially exchangeable and only desorb from a surface in response to compression or change in composition. Here, we develop a thermodynamic and kinetic model to describe this phenomenon based on the change in the interfacial pressure (Π) of the C-terminal 46 amino acids of apolipoprotein A-I (C46) at a TO/W interface. This model suggests that apolipoproteins have at least two interfacial conformations that are in a surface concentration and Π-dependent equilibrium. This two-state surface equilibrium model, which is based on experimental data and is consistent with dynamic changes in Π(t), provides insights into the selective metabolism and clearance of plasma lipoproteins and the process of lipoprotein remodeling.

AB - Amphipathic α-helices (AαH) are the primary structural motif of exchangeable apolipoproteins. AαHs in exchangeable apolipoproteins adsorb, remodel, and desorb at the surface of plasma lipoproteins in response to changes in their size or composition. A triolein/water (TO/W) interface was used as a model surface to study adsorption and desorption of AαHs at a lipoprotein-like interface. We previously reported that AαH peptides spontaneously adsorb to a TO/W interface, but they only partially desorb from the surface when the excess peptide was removed from the system. This finding suggests that "exchangeable" apolipoproteins are in fact partially exchangeable and only desorb from a surface in response to compression or change in composition. Here, we develop a thermodynamic and kinetic model to describe this phenomenon based on the change in the interfacial pressure (Π) of the C-terminal 46 amino acids of apolipoprotein A-I (C46) at a TO/W interface. This model suggests that apolipoproteins have at least two interfacial conformations that are in a surface concentration and Π-dependent equilibrium. This two-state surface equilibrium model, which is based on experimental data and is consistent with dynamic changes in Π(t), provides insights into the selective metabolism and clearance of plasma lipoproteins and the process of lipoprotein remodeling.

KW - Apolipoproteins

KW - Lipoprotein remodeling

KW - Protein-lipid interactions

UR - http://www.scopus.com/inward/record.url?scp=84877884853&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84877884853&partnerID=8YFLogxK

U2 - 10.1194/jlr.M034462

DO - 10.1194/jlr.M034462

M3 - Article

C2 - 23528259

AN - SCOPUS:84877884853

VL - 54

SP - 1578

EP - 1588

JO - Journal of Lipid Research

JF - Journal of Lipid Research

SN - 0022-2275

IS - 6

ER -