AI Article Synopsis
- Detergents used for solubilizing integral membrane proteins (IMPs) can destabilize proteins and reduce their activity, presenting a challenge in membrane protein research.
- Alternative systems like lipid nanodiscs (NDs) and saposin-lipoprotein particles (Salipro) provide a more stable, native-like environment for studying these proteins.
- A study comparing NDs and Salipros using the ABC transporter MsbA showed both systems effectively maintain protein activity and stability, suggesting that different lipids should be tested for optimal results before structural analysis.
Article Abstract
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. Our results show that both systems are suitable for activity measurements as well as structural studies in solution. Based on our results we suggest screening of different lipids with respect to activity and stability of the incorporated IMP before performing structural studies.
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| http://dx.doi.org/10.1515/hsz-2019-0171 | DOI Listing |
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