Skip to Main content Skip to Navigation
Journal articles

New tensio-active molecules stabilize a human G protein-coupled receptor in solution.

Abstract : Structural characterization of membrane proteins is hampered by the instability of the isolated proteins in detergent solutions. Here, we describe a new class of phospholipid-like surfactants that stabilize the G protein-coupled receptor, BLT1. These compounds, called C(13)U(9), C(13)U(19), C(15)U(25) and C(17)U(16), were synthesized by radical polymerization of Tris(hydroxymethyl) acrylamidomethane in the presence of thioglycerol, first endowed with two hydrocarbon chains with variable lengths (13-17 carbon atoms), as transfer reagent. C(13)U(19), C(17)U(16) or C(15)U(25) significantly enhanced the stability of BLT1 in solution compared to what was obtained with common detergents. These molecules therefore represent a promising step towards the structural characterization of BLT1 and possibly other membrane proteins.
Document type :
Journal articles
Complete list of metadata

Cited literature [28 references]  Display  Hide  Download
Contributor : Isabelle Arnal Connect in order to contact the contributor
Submitted on : Tuesday, October 1, 2013 - 4:50:08 PM
Last modification on : Friday, August 5, 2022 - 10:36:57 AM
Long-term archiving on: : Friday, April 7, 2017 - 4:43:35 AM


 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document




Marjorie Damian, Sandrine Perino, Ange Polidori, Aimée Martin, Laurence Serre, et al.. New tensio-active molecules stabilize a human G protein-coupled receptor in solution.. FEBS Letters, Wiley, 2007, 581 (10), pp.1944-50. ⟨10.1016/j.febslet.2007.03.091⟩. ⟨inserm-00868640⟩



Record views