The influence of heptane-1,2,3-triol on the size and shape of LDAO micelles Implications for the crystallisation of membrane proteins

• Published in: FEBS letters 1991-03, Vol.280 (1), p.115-120
• Main Authors: Timmins, Peter A., Hauk, Jürgen, Wacker, Thomas, Welte, Wolfram
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Dimethylamines; Fatty Alcohols - metabolism; Fundamental and applied biological sciences. Psychology; lauryldimethyl amine oxide; Membrane protein crystallization; membrane proteins; Membrane Proteins - chemistry; Micelles; Miscellaneous; Mixed micelles; neutron scattering; Neutrons; Proteins; Small amphiphiles; Small angle neutron scattering; Surfactant micelles; X-Ray Diffraction
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(91)80217-Q

The presence of small amphiphiles has been found to be necessary in the crystallization of several membrane-protein surfactant complexes. It has been suggested that the role of the small amphiphile may be to reduce the size of the surfactant belt around the protein, making the formation of crystals easier. Thus far it was not known if this would involve changes in micellar size in general or whether the small amphiphile would merely replace LDAO during crystal growth. In the present study we have used small angle neutron scattering to study mixed micelles of lauryldimethyl amine oxide (LDAO; hydrogenated and deuterated) and heptane-1,2,3-triol (HP). Our results show that with increasing overall HP concentrations mixed LDAO/HP micelles of decreasing mass and radius are formed. The composition of these micelles has been determined. HP thus may decrease the size of the surfactant belt around a protein before crystallisation by insertion into a host micelle. As HP is a ‘small amphiphile’ compared to the surfactants used for solubilization of membrane proteins, the curvature of the host micelle will be increased by its insertion.