The development of new, targeted drugs relies heavily on innovative technologies that allow for high-throughput screening of drug libraries against biologically relevant targets, particularly membrane-associated receptors. Therefore, immobilization of natural receptors is of the utmost importance to allow for screening of small molecule libraries. Herein, we describe the immobilization of liposomes containing the transmembrane peptide ion-channel gramicidin A into sol-gel-derived silicate materials. Steady-state fluorescence measurements of the intrinsic tryptophan residues of reconstituted gramicidin A in phospholipid vesicles consisting of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) were obtained in solution and following entrapment in diglyceryl silane (DGS)-derived silicate to examine the effects of entrapment on the conformation of the ion channel. Only minor deviations were observed in the fluorescence properties of gramicidin following entrapment in DGS-derived silicate. DOPC vesicles containing a 50 microM internal solution of the potential sensitive fluorescent dye safranine O were used to study ion flux through the membrane ion channel. The dependence of ion flux on both ion concentration and amount of gramicidin embedded in the membrane were examined before and after entrapment in sol-gel-derived silicate. It was found that ion channel activity upon entrapment in DGS-derived silicate mirrored very closely that observed in solution. Moreover, the ability to inhibit ion flux through gramicidin A due to blockage by calcium ions was retained after the immobilization procedure. The implications for development of drug-screening and -sensing platforms are discussed.