Protein Science Attend a BioResearch Product Faire
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Duval-Terrié, C.
Right arrow Articles by Dé, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Duval-Terrié, C.
Right arrow Articles by Dé, E.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
Protein Science (2003), 12:681-689.
Copyright © 2003 The Protein Society

Amphiphilic biopolymers (amphibiopols) as new surfactants for membrane protein solubilization

Caroline Duval-Terrié1, Pascal Cosette1, Gérard Molle2, Guy Muller1 and Emmanuelle Dé2

1 Laboratoire Polymères, Biopolymères, Membranes, Unité Mixte de Recherche 6522 (CNRS et Université de Rouen), F-76 821 Mont Saint Aignan Cedex, France
2 Centre de Biochimie Structurale, Unité Mixte de Recherche 5048 CNRS et 554 INSERM, F-34 090 Montpellier, France

Reprint requests to: Emmanuelle Dé, Laboratoire Polymères, Biopolymères, Membranes, UMR 6522 CNRS, Université de Rouen, F-76 821 Mont Saint Aignan Cedex, France; e-mail: emmanuelle.de{at}univ-rouen.fr; fax: 33-2-3514-6704.

The aim of this study was to develop new surfactants for membrane protein solubilization, from a natural, biodegradable polymer: the polysaccharide pullulan. A set of amphiphilic pullulans (HMCMPs), differing in hydrophobic modification ratio, charge ratio, and the nature of the hydrophobic chains introduced, were synthesized and tested in solubilization experiments with outer membranes of Pseudomonas fluorescens. The membrane proteins were precipitated, and then resolubilized with various HMCMPs. The decyl alkyl chain (C10) was the hydrophobic graft that gave the highest level of solubilization. Decyl alkyl chain-bearing HMCMPs were also able to extract integral membrane proteins from their lipid environment. The best results were obtained with an amphiphilic pullulan bearing 18% decyl groups (18C10). Circular dichroism spectroscopy and membrane reconstitution experiments were used to test the structural and functional integrity of 18C10-solubilized proteins (OmpF from Escherichia coli and bacteriorhodopsin from Halobacterium halobium). Whatever their structure type ({alpha} or ß), 18C10 did not alter either the structure or the function of the proteins analyzed. Thus, HMCMPs appear to constitute a promising new class of polymeric surfactants for membrane protein studies.

Keywords: Membrane protein; solubilization; amphiphilic polysaccharide; polymeric surfactant; pullulan

Abbreviations: BR, bacteriorhodopsin • HMCMP, hydrophobically modified carboxymethylpullulan • LiDS, lithium dodecylsulfate • Octyl-POE, octylpolyoxyethylene • Tris-HCl, Tris(hydroxymethyl)aminomethane hydrochloride


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Protein Sci.Home page
M. Picard, C. Duval-Terrie, E. De, and P. Champeil
Stabilization of membranes upon interaction of amphipathic polymers with membrane proteins
Protein Sci., November 1, 2004; 13(11): 3056 - 3058.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2003 by The Protein Society.