Abstract:
:We examined model mixed micelles consisting of the nonionic surfactant n-dodecyl-β-D-maltoside, 3-(3-cholamidopropyl)-dimethylammoniopropane sulfonate, and the cholesterol derivative cholesteryl hemisuccinate (CHS) to identify micellar properties that are correlated with the in vitro conformational stability and activity of the human adenosine A₂a receptor, a G-protein coupled receptor. Small-angle neutron scattering was used to determine micellar structure and composition as a function of concentration of the various components, and radioligand binding was used as a sensitive probe for receptor activity. Micelles adopted an oblate ellipsoidal morphology and exhibited a reduction in size and change in curvature upon addition of CHS. Our results show a strong correlation between the number of CHS monomers per micelle and the activity of the receptor reconstituted in those micelles. Micelles that yield optimal human adenosine A₂a receptor stability closely mimic the cholesterol composition and thickness of mammalian membranes. Thus, successful reconstitution of the receptor is dependent on both specific lipid-protein interactions and the geometry of the micelle environment.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
O'Malley MA,Helgeson ME,Wagner NJ,Robinson ASdoi
10.1016/j.bpj.2010.12.3698subject
Has Abstractpub_date
2011-01-19 00:00:00pages
L11-3issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(10)05214-8journal_volume
100pub_type
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