Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface

Viscoelastic behavior of proteins at interfaces is a critical determinant of their ability to stabilize emulsions. We therefore used air bubble surfactometry and drop volume tensiometry to examine the dynamic interfacial properties of two plasma apolipoproteins involved in chylomicron assembly: apol...

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Main Authors: Richard B. Weinberg, Victoria R. Cook, Jeanine A. DeLozier, Gregory S. Shelness
Format: Article
Language:English
Published: Elsevier 2000-09-01
Series:Journal of Lipid Research
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520334544
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spelling doaj-37c4d6383c9b4e74b5a96115c71d521c2021-04-27T04:45:05ZengElsevierJournal of Lipid Research0022-22752000-09-0141914191427Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interfaceRichard B. Weinberg0Victoria R. Cook1Jeanine A. DeLozier2Gregory S. Shelness3Section of Gastroenterology, Department of Internal Medicine, Wake Forest University School of Medicine, Winston-Salem, NC 27157; To whom correspondence should be addressed.Section of Gastroenterology, Department of Internal Medicine, Wake Forest University School of Medicine, Winston-Salem, NC 27157Section of Comparative Medicine, Department of Pathology, Wake Forest University School of Medicine, Winston-Salem, NC 27157Section of Comparative Medicine, Department of Pathology, Wake Forest University School of Medicine, Winston-Salem, NC 27157Viscoelastic behavior of proteins at interfaces is a critical determinant of their ability to stabilize emulsions. We therefore used air bubble surfactometry and drop volume tensiometry to examine the dynamic interfacial properties of two plasma apolipoproteins involved in chylomicron assembly: apolipoprotein A-IV and apolipoprotein B-17, a recombinant, truncated apolipoprotein B. At the air/water interface apolipoproteins A-IV and B-17 displayed wide area-tension loops with positive phase angles indicative of viscoelastic behavior, and suggesting that they undergo rate-dependent changes in surface conformation in response to changes in interfacial area. At the triolein/water interface apolipoprotein A-IV displayed maximal surface activity only at long interface ages, with an adsorption rate constant of 1.0 × 10−3 sec−1, whereas apolipoprotein B-17 lowered interfacial tension even at the shortest interface ages, with an adsorption rate constant of 9.3 × 10−3 sec−1. Apolipoprotein A-IV displayed an expanded conformation at the air/water interface and a biphasic compression isotherm, suggesting that its hydrophilic amphipathic helices move in and out of the interface in response to changes in surface pressure. We conclude that apolipoproteins A-IV and B-17 display a combination of interfacial activity and elasticity particularly suited to stabilizing the surface of expanding triglyceride-rich particles. —Weinberg, R. B., V. R. Cook, J. A. DeLozier, and G. S. Shelness. Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface. J. Lipid Res. 2000. 41: 1419–1427.http://www.sciencedirect.com/science/article/pii/S0022227520334544surface tensioninterfacial elasticitydrop volume tensiometrychylomicron assemblycholesterolmonolayers
collection DOAJ
language English
format Article
sources DOAJ
author Richard B. Weinberg
Victoria R. Cook
Jeanine A. DeLozier
Gregory S. Shelness
spellingShingle Richard B. Weinberg
Victoria R. Cook
Jeanine A. DeLozier
Gregory S. Shelness
Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface
Journal of Lipid Research
surface tension
interfacial elasticity
drop volume tensiometry
chylomicron assembly
cholesterol
monolayers
author_facet Richard B. Weinberg
Victoria R. Cook
Jeanine A. DeLozier
Gregory S. Shelness
author_sort Richard B. Weinberg
title Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface
title_short Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface
title_full Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface
title_fullStr Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface
title_full_unstemmed Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface
title_sort dynamic interfacial properties of human apolipoproteins a-iv and b-17 at the air/water and oil/water interface
publisher Elsevier
series Journal of Lipid Research
issn 0022-2275
publishDate 2000-09-01
description Viscoelastic behavior of proteins at interfaces is a critical determinant of their ability to stabilize emulsions. We therefore used air bubble surfactometry and drop volume tensiometry to examine the dynamic interfacial properties of two plasma apolipoproteins involved in chylomicron assembly: apolipoprotein A-IV and apolipoprotein B-17, a recombinant, truncated apolipoprotein B. At the air/water interface apolipoproteins A-IV and B-17 displayed wide area-tension loops with positive phase angles indicative of viscoelastic behavior, and suggesting that they undergo rate-dependent changes in surface conformation in response to changes in interfacial area. At the triolein/water interface apolipoprotein A-IV displayed maximal surface activity only at long interface ages, with an adsorption rate constant of 1.0 × 10−3 sec−1, whereas apolipoprotein B-17 lowered interfacial tension even at the shortest interface ages, with an adsorption rate constant of 9.3 × 10−3 sec−1. Apolipoprotein A-IV displayed an expanded conformation at the air/water interface and a biphasic compression isotherm, suggesting that its hydrophilic amphipathic helices move in and out of the interface in response to changes in surface pressure. We conclude that apolipoproteins A-IV and B-17 display a combination of interfacial activity and elasticity particularly suited to stabilizing the surface of expanding triglyceride-rich particles. —Weinberg, R. B., V. R. Cook, J. A. DeLozier, and G. S. Shelness. Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface. J. Lipid Res. 2000. 41: 1419–1427.
topic surface tension
interfacial elasticity
drop volume tensiometry
chylomicron assembly
cholesterol
monolayers
url http://www.sciencedirect.com/science/article/pii/S0022227520334544
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