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- W4205324871 abstract "Abstract Outer membrane proteins (OMPs), located on the outer membrane of gram-negative bacteria, have a β-strand structure and form nanopores, which allow passage of ions, sugars, and small molecules. Recently, OMPs have been used as sensing elements to detect biological molecules. OMPs are normally expressed and purified from E. coli.. Although the cell-free synthesis of OMPs, such as OmpA and OmpG, is achieved in the presence of liposomes and periplasmic chaperones, the amount of OmpA and OmpG incorporated into the nano-sized liposomes is not clear. In this study, after in vitro translation, the incorporation of OmpG into purified nano-sized liposomes, with various lipid compositions, was investigated. Liposomes containing the synthesized OmpG were purified using a stepwise sucrose density gradient. We report that liposomes prepared with the E. coli lipid extract (PE/PG) had the highest amount of OmpG incorporated compared to liposomes with other lipid compositions, as detected by recording the current across the OmpG containing liposomes using the patch clamp technique. This study reveals some of the requirements for the insertion and refolding of OMPs synthesized by the in vitro translation system into lipid membranes, which plays a role in the biological sensing of various molecules." @default.
- W4205324871 created "2022-01-26" @default.
- W4205324871 creator A5030492673 @default.
- W4205324871 date "2021-10-22" @default.
- W4205324871 modified "2023-10-16" @default.
- W4205324871 title "Formation and function of bacterial outer membrane proteins- incorporated liposomes using an in vitro translation system" @default.
- W4205324871 doi "https://doi.org/10.21203/rs.3.rs-964946/v1" @default.
- W4205324871 hasPublicationYear "2021" @default.
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