Amphipols: Polymeric surfactants for membrane biology research

Popot, J-L., Berry, E. A., Charvolin, D., Creuzenet, C., Ebel, C., Engelman, D. M., Floetenmeyer, M., Giusti, F., Gohon, Y., Hong, Q., Lakey, J. H., Leonard, K., Shuman, H. A., Timmins, P., Warschawki, D. E., Zito, F., Zonnens, M., Pucci, B. and Tribet, C. (2003) Amphipols: Polymeric surfactants for membrane biology research. Cellular and Molecular Life Sciences, 60 8: 1559-1574. doi:10.1007/s00018-003-3169-6

Author Popot, J-L.
Berry, E. A.
Charvolin, D.
Creuzenet, C.
Ebel, C.
Engelman, D. M.
Floetenmeyer, M.
Giusti, F.
Gohon, Y.
Hong, Q.
Lakey, J. H.
Leonard, K.
Shuman, H. A.
Timmins, P.
Warschawki, D. E.
Zito, F.
Zonnens, M.
Pucci, B.
Tribet, C.
Title Amphipols: Polymeric surfactants for membrane biology research
Journal name Cellular and Molecular Life Sciences   Check publisher's open access policy
ISSN 1420-682X
Publication date 2003
Year available 2004
Sub-type Article (original research)
DOI 10.1007/s00018-003-3169-6
Volume 60
Issue 8
Start page 1559
End page 1574
Total pages 16
Editor K. Eichmann
Place of publication Basel, Switzerland
Publisher Birkhauser Verlag AG
Collection year 2004
Language eng
Subject 060112 Structural Biology (incl. Macromolecular Modelling)
Abstract Membrane proteins classically are handled in aqueous solutions as complexes with detergents. The dissociating character of detergents, combined with the need to maintain an excess of them, frequently results in more or less rapid inactivation of the protein under study. Over the past few years, we have endeavored to develop a novel family of surfactants, dubbed amphipols (APs). APs are amphiphilic polymers that bind to the transmembrane surface of the protein in a noncovalent but, in the absence of a competing surfactant, quasi-irreversible manner. Membrane proteins complexed by APs are in their native state, stable, and they remain water-soluble in the absence of detergent or free APs. An update is presented of the current knowledge about these compounds and their demonstrated or putative uses in membrane biology.
Keyword Membrane proteins
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Centre for Microscopy and Microanalysis Publications
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Citation counts: TR Web of Science Citation Count  Cited 119 times in Thomson Reuters Web of Science Article | Citations
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Created: Thu, 08 Jan 2009, 10:29:09 EST by Maryanne Watson on behalf of Centre for Microscopy and Microanalysis