184872-75-1Relevant academic research and scientific papers
Detergent-Like Polymerizable Monomers: Synthesis, Physicochemical, and Biochemical Characterization
Bonnet, Christophe,Durand, Grégory,Guillet, Pierre,Igonet, Sébastien,Jawhari, Anass,Keller, Sandro,Mahler, Florian
, (2020)
Three monomers with a maltose polar head, an alkyl hydrogenated chain, and an acrylamide-based polymerizable moiety were synthesized. The self-assembly properties in aqueous solutions of these monomers were studied by means of isothermal titration calorimetry (ITC), surface tension (SFT) measurements, and dynamic light scattering (DLS), which indicated the formation of small micellar aggregates of about 6 nm diameter. The critical micellar concentration (CMC) was found to depend on the length of the alkyl chain and on the nature of the polymerizable moiety, ranging from 0.35 mm to ca. 10 mm. The monomers were found to solubilize phospholipid vesicles and to extract a broad range of proteins from Escherichia coli membranes. Finally, the extraction of two membrane proteins, namely, the full-length, wild-type human G-protein-coupled receptor (GPCR) adenosine A2A receptor (A2AR) and the bacterial transporter AcrB was demonstrated.
Hybrid double-chain maltose-based detergents: Synthesis and colloidal and biochemical evaluation
Bonnet, Christophe,Guillet, Pierre,Igonet, Sébastien,Meister, Annette,Marconnet, Ana?s,Keller, Sandro,Jawhari, Anass,Durand, Grégory
, p. 10606 - 10614 (2019)
Four hybrid double-chain surfactants with a maltose polar head were synthesized. The apolar domain consists of a hydrogenated chain, and a partially fluorinated chain made of a propyl hydrogenated spacer terminated by a perfluorinated core of various leng
Microscale NMR screening of new detergents for membrane protein structural biology
Zhang, Qinghai,Horst, Reto,Geralt, Michael,Ma, Xingquan,Hong, Wen-Xu,Finn,Stevens, Raymond C.,Wuethrich, Kurt
, p. 7357 - 7363 (2008/12/21)
The rate limiting step in biophysical characterization of membrane proteins is often the availability of suitable amounts of protein material. It was therefore of interest to demonstrate that microcoil nuclear magnetic resonance (NMR) technology can be used to screen microscale quantities of membrane proteins for proper folding in samples destined for structural studies. Micoscale NMR was then used to screen a series of newly designed zwitterionic phosphocholine detergents for their ability to reconstitute membrane proteins, using the previously well characterized β-barrel E. coli outer membrane protein OmpX as a test case. Fold screening was thus achieved with microgram amounts of uniformly 2H,15N-labeld OmpX and affordable amounts of the detergents, and prescreening with SDS-gel electrophoresis ensured efficient selection of the targets for NMR studies. A systematic approach to optimize the phosphocholine motif for membrane protein refolding led to the identification of two new detergents, 138-Fos and 179-Fos, that yield 2D [ 15N,1H]-TROSY correlation NMR spectra of natively folded reconstituted OmpX.
