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Integration of Ganglioside GT_1b Receptor into DPPE and DPPC Phospholipid Monolayers: An X-Ray Reflectivity and Grazing-Incidence Diffraction Study

C. E. Miller ^*, D. D. Busath , B. Strongin  and J. Majewski ^*

^* Manuel Lujan Neutron Scattering Center, Los Alamos National Laboratory, Los Alamos, New Mexico, and Department of Physiology and Developmental Biology, Brigham Young University, Provo, Utah

Correspondence: Address reprint requests to J. Majewski, Lujan Neutron Scattering Center, Los Alamos National Laboratory, Los Alamos, New Mexico. E-mail: jarek{at}lanl.gov.

Using synchrotron grazing-incidence x-ray diffraction (GIXD) and reflectivity, the in-plane and out-of-plane structures of mixed-ganglioside GT_1b-phospholipid monolayers were investigated at the air-liquid interface and compared with monolayers of the pure components. The receptor GT_1b is involved in the binding of lectins and toxins, including botulinum neurotoxin, to cell membranes. Monolayers composed of 20 mol % ganglioside GT_1b, the phospholipid dipalmitoyl phosphatidylethanolamine (DPPE), and the phospholipid dipalmitoyl phosphatidylcholine (DPPC) were studied in the gel phase at 23°C and at surface pressures of 20 and 40 mN/m, and at pH 7.4 and 5. Under these conditions, the two components did not phase-separate, and no evidence of domain formation was observed. The x-ray scattering measurements revealed that GT_1b was intercalated within the host DPPE/DPPC monolayers, and slightly expanded DPPE but condensed the DPPC matrix. The oligosaccharide headgroups extended normally from the monolayer surfaces into the subphase. This study demonstrated that these monolayers can serve as platforms for investigating toxin membrane binding and penetration.