Out now: ABC transporters like lipids - so do we! The second publication on an active ABC transporter in Salipro® in a month - this time from the Tidow lab in Hamburg, Germany - link to publication : https://www.degruyter.com/view/j/bchm.ahead-of-print/hsz-2019-0171/hsz-2019-0171.xml
Membrane protein research suffers from the drawback that detergents, which are commonly used to solubilize integral membrane proteins (IMPs), often lead to protein instability and reduced activity. Recently, lipid nanodiscs (NDs) and saposin-lipoprotein particles (Salipro) have emerged as alternative carrier systems that keep membrane proteins in a native-like lipidic solution environment and are suitable for biophysical and structural studies. Here, we systematically compare nanodiscs and Salipros with respect to long-term stability as well as activity and stability of the incorporated membrane protein using the ABC transporter MsbA as model system.
Salipro® in Japan! Congratulations to the Takagi and Nureki labs on the 4.1 Å cryoEM structure of a MFS transporter - 56 transmembrane helices in a lipid Salipro® environment. Find out more in the recent publication:
Find out more in the recent publication of the Schmitt lab: “We conclude that the Salipro-system is a seminal approach not only for structural, but also for the functional characterisation of membrane proteins.”
Title: Functional Reconstitution of HlyB, a Type I Secretion ABC Transporter, in Saposin-A Nanoparticles - Kerstin Kanonenberg, Sander H. J. Smits & Lutz Schmitt - Sci Rep. 2019 Jun 10;9(1):8436. doi: 10.1038/s41598-019-44812-0.
Link to publication >click here<
Here, we present DirectMX™ (link) for the direct extraction of membrane proteins from crude cell membranes into Salipro® particles with native lipids. The method presents new opportunities for the analysis of membrane proteins and identification of novel drug targets.
Contact us directly if you are interested in this recent application note.