The goal of the proposed research is to prepare and characterize novel polymeric phospholipid bilayer assemblies as substrates for protein attachment. Immobilization of protein receptors on the bilayer surface has important practical applications for the development of new biosensors utilizing the bound protein as the biologically selective recognition element. The implementation of lipid bilayers as substrates for protein immobilization and subsequent use as biosensors requires that the chemical and structural properties be improved while maintaining the low nonspecific binding properties of lipid bilayer. The strategy to be investigated here is the lateral polymerization of the phospholipid bilayer in conjunction with site directed immobilization of proteins on the surface. The proposed research will involve preparation and characterization of novel tethered planar polymer phospholipid bilayers. The stability of the prepared cross- linked polymer phospholipid bilayers will then be assessed by solubility and optical measurements. The polymer lipid bilayers will subsequently be utilized as substrates for site directed protein immobilization. The proposed research will attempt to discern if the low nonspecific adsorption characteristic of fluid lipid bilayer are preserved upon cross-linking of the lipid bilayer and covalent attachment to the substrate. The resulting assembly should result in a stable protein- lipid assembly with an oriented presentation of the adsorbed protein film with maximum retention of protein structure and function.
| Conboy, John C; McReynolds, Katherine D; Gervay-Hague, Jacquelyn et al. (2002) Quantitative measurements of recombinant HIV surface glycoprotein 120 binding to several glycosphingolipids expressed in planar supported lipid bilayers. J Am Chem Soc 124:968-77 |
