help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Originally published as Biophys J. BioFAST on November 9, 2007.
doi:10.1529/biophysj.107.115220
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
biophysj.107.115220v1
94/5/1735    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bolanos-Garcia, V. M.
Right arrow Articles by Beaufils, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bolanos-Garcia, V. M.
Right arrow Articles by Beaufils, S.
Biophysical Journal 94:1735-1745 (2008)
© 2008 The Biophysical Society

Surface Rheology and Adsorption Kinetics Reveal the Relative Amphiphilicity, Interfacial Activity, and Stability of Human Exchangeable Apolipoproteins

Victor Martin Bolanos-Garcia *, Anne Renault {dagger} and Sylvie Beaufils {dagger}

* Department of Biochemistry, University of Cambridge, Cambridge CB2 1TN, United Kingdom; and {dagger} Groupe Matiere Condensee et Materiaux, Universite de Rennes 1, Campus de Beaulieu, 35042 Rennes cedex, France

Correspondence: Address reprints requests to Sylvie Beaufils, Université de Rennes 1. Bat 11A, Campus Beaulieu, 35042 Rennes cedex, France. E-mail: sylvie.beaufils{at}univ-rennes1.fr.

Exchangeable apolipoproteins are located in the surface of lipoprotein particles and regulate lipid metabolism through direct protein-protein and protein-lipid interactions. These proteins are characterized by the presence of tandem repeats of amphiphatic {alpha}-helix segments and a high surface activity in monolayers and lipoprotein surfaces. A noteworthy aspect in the description of the function of exchangeable apolipoproteins is the requirement of a quantitative account of the relation between their physicochemical and structural characteristics and changes in the mesoscopic system parameters such as the maximum surface pressure and relative stability at interfaces. To comply with this demand, we set out to establish the relations among {alpha}-helix amphiphilicity, surface concentration, and surface rheology of apolipoproteins ApoA-I, ApoA-II, ApoC-I, ApoC-II, and ApoC-III adsorbed at the air-water interface. Our studies render further insights into the interfacial properties of exchangeable apolipoproteins, including the kinetics of their adsorption and the physical properties of the interfacial layer.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2008 by the Biophysical Society.