Journal
NANOSCALE
Volume 10, Issue 22, Pages 10609-10619Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8nr01322e
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Funding
- Engineering and Physical Sciences Research Council [EPSRC: EP/M506461/1]
- Diamond Light Source studentship
- Biotechnology and Biological Sciences Research Council [BBSRC: BB/M018261/1, BB/J017310/1, BB/1020349/1, BB/P009840/1, BB/L00335X/1]
- STFC BioMedNet [2990]
- University of Bath
- Medical Research Council (MRC)
- AstraZeneca
- University of Bristol
- BBSRC [BB/P009840/1, BB/I020349/1, BB/M018261/1, BB/J017310/1] Funding Source: UKRI
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The fundamental importance of membrane proteins in drug discovery has meant that membrane mimetic systems for studying membrane proteins are of increasing interest. One such system has been the amphipathic, negatively charged poly(styrene-co-maleic acid) (SMA) polymer to form SMA Lipid Particles (SMALPs) which have been widely adopted to solubilize membrane proteins directly from the cell membrane. However, SMALPs are only soluble under basic conditions and precipitate in the presence of divalent cations required for many downstream applications. Here, we show that the positively charged poly(styrene-co-maleimide) (SMI) forms similar nanoparticles with comparable efficiency to SMA, whilst remaining functional at acidic pH and compatible with high concentrations of divalent cations. We have performed a detailed characterization of the performance of SMI that enables a direct comparison with similar data published for SMA. We also demonstrate that SMI is capable of extracting proteins directly from the cell membrane and can solubilize functional human G-protein coupled receptors (GPCRs) expressed in cultured HEK 293T cells. SMILPs thus provide an alternative membrane solubilization method that successfully overcomes some of the limitations of the SMALP method.
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