小角X射线散射
膜
膜蛋白
化学
肽
磷脂
生物物理学
跨膜蛋白
小角中子散射
脂质双层
纳米圆盘
中子散射
结晶学
散射
生物化学
受体
生物
物理
光学
作者
Søren Roi Midtgaard,Martin Cramer Pedersen,Jacob J. K. Kirkensgaard,Kasper K. Sørensen,K. Mortensen,Knud J. Jensen,Lise Arleth
出处
期刊:Soft Matter
[The Royal Society of Chemistry]
日期:2014-01-01
卷期号:10 (5): 738-752
被引量:64
摘要
New methods to handle membrane bound proteins, e.g. G-protein coupled receptors (GPCRs), are highly desirable. Recently, apoliprotein A1 (ApoA1) based lipoprotein particles have emerged as a new platform for studying membrane proteins, and it has been shown that they can self-assemble in combination with phospholipids to form discoidal shaped particles that can stabilize membrane proteins. In the present study, we have investigated an ApoA1 mimetic peptide with respect to its solution structure when in complex with phospholipids. This was achieved using a powerful combination of small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) supported by coarse-grained molecular dynamics simulations. The detailed structure of the discs was determined in unprecedented detail and it was found that they adopt a discoidal structure very similar to the ApoA1 based nanodiscs. We furthermore show that, like the ApoA1 and derived nanodiscs, these peptide discs can accommodate and stabilize a membrane protein. Finally, we exploit their dynamic properties and show that the 18A discs may be used for transferring membrane proteins and associated phospholipids directly and gently into phospholipid nanodiscs.
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