Novel zwitterionic reverse micelles for encapsulation of proteins in low-viscosity media.
Large proteins remain inaccessible to structural NMR studies because of their unfavorable relaxation properties. Their solubilization in the aqueous core of reverse micelles, in a low-viscosity medium, represents a promising approach, provided that their native tertiary structure is maintained. However, the use of classical ionic surfactants may lead to protein unfolding, due to strong electrostatic interactions between the polar head groups and the protein charges. To design reverse micelles in which these interactions are weakened, a new zwitterionic surfactant molecule was synthesized and studied by high-resolution NMR spectroscopy, for which cytochrome C and 15N-labeled ubiquitin were used as guest candidates. At different ionization states, both proteins are encapsulated in the absence of salts or other additives, in a folded conformation similar to the native one.
Laboratoire Structure et Dynamique par Résonance Magnétique, DSM/DRECAM/Service de Chimie Moléculaire, URA CEA/CNRS 331, CEA/Saclay, 91191 Gif sur Yvette, France.
Sylvain
S
Doussin
Nicolas
N
Birlirakis
Dominique
D
Georgin
Frédéric
F
Taran
Patrick
P
Berthault
D008823:Micelles; D011506:Proteins / Q000737:chemistry*; D014783:Viscosity
D008823:Micelles; D011506:Proteins