For the development of new therapies or preventive strategies, it is mandatory to have membrane proteins (GPCR, ion channels, viral envelope proteins …) in the purest form but still in native conformation and integrated into a membrane.
Unlike soluble proteins that are fairly easy to produce in their native conformation, this is very difficult for integral membrane proteins. They rely on mutually incompatible environments, ie “aqueous-lipid-aqueous”. The influence of membrane phospholipids on membrane proteins conformation is also particularly significant. In the absence of such specific environments, the membrane proteins do not fold properly and therefore are not functional.
In addition, most membrane proteins must acquire specific post-translational modifications for correct folding and several are active as homo- or hetero-oligomers. These highly complex and fragile proteins are altered when extracted according to current methods.