About half of known bioactive organic molecules, including drugs, are known to target biological membranes and membrane proteins. Despite this, it has proven difficult to define the membrane-bound conformations of these molecules. In recent years, bicelles have been recognized as a more appropriate membrane model than micelles because their planar portion is composed of a lipid bilayer. Bicelles with a small diameter, termed isotropic or fast-tumbling bicelles, allow for high-resolution NMR measurements due to their high mobility in suspension, and therefore have become a versatile tool for structure studies of membrane-associated molecules. Following a brief description of the morphology and preparation of isotropic bicelles, we summarize their application to structural studies of membrane-bound peptides and small molecules, and then highlight our recent studies on the 3D structures of erythromycin A, salinomycin and amphidinol 3 using isotropic bicelles.
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