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Abstract: We have recently developed (Proc. Natl. Acad. Sci. USA 87, 274 (1990)) a methodology for transforming common proteins into selective artificial receptors. This strategy utilizes the phenomenon of drastically lowered protein flexibility in anhydrous organic solvents (compared to water) in order to create (or enhance) protein-ligand interactions in non-aqueous media. By lyophilizing a protein from an aqueous solution in the presence of a ligand, followed by removal of the latter (via washing with anhydrous organic solvent), the resultant "imprinted" protein exhibits a much greater capacity to bind the print molecule in anhydrous media than the nonimprinted protein or either protein in water. We have succeeded in imprinting several unrelated proteins with a variety of organic compounds. The dependence of this effect on the structures the print molecule and the protein, solvent, and the conditions of imprinting will be discussed. The application of these novel receptors as unique bioadsorbents will also be addressed.