Refolding of the outer membrane PagP from an original surfactant-based method
Membrane proteins (MPs) are important therapeutic targets and of biotechnological relevance because they can improve the performance of biomaterials. However, studying MPs in vitro is challenging, because it implies their overexpression under a functional form. The development of new efficient refolding techniques is urgently awaited in this field. In that context, we have first shown that specific amphipathic cosolvents such as 2-Methyl-2,4-PentaneDiol (MPD) is able to protect proteins from Sodium Dodecyle Sulfate (SDS) denaturation, and can refold proteins from the SDS-denatured state. Several types of MPs were already refolded by using this method. Our general objective is to understand the molecular basis of the particular assembly between SDS and MPD in order to improve its efficiency. In the present project, we would like to investigate the refolding of a model MP, PagP, from the SDS-MPD protocol. First, several d-MPD and d-SDS concentrations will be assayed to follow the refolding of PagP. Then, a similar experiment will be performed but highlighting SDS. It will provide information on the degree of SDS-protein association as a function of d-MPD concentrations.
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MICHAUX Catherine; MARTEL Anne; E.A. Perpète and PORCAR Lionel. (2019). Refolding of the outer membrane PagP from an original surfactant-based method. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-815
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