(216y) Asymmetric Recognition of L-/-Amino Acid By Liposome Membrane

Liposome membrane is a self-assembly of the phospholipid molecules prepared in water and can be regarded as a model biomembrane. Recent research shows the possibility of the chiral recognition function of the liposome membrane through the binding of the dipeptide on the liposome membrane. The purpose of this study is development of new optical resolution method by using liposome membrane. We first investigated the chiral recognition function of liposome membrane by observing the adsorption of amino acids that have different chirality. We also investigated the ability of optical resolution by using equilibrium dialysis method with hydrogel entrapping liposome membranes. The adsorption of L-Trp on the DPPC liposome membrane was increased with the incubation time and the value was reached to approximately 100% in more than 48 hours, while that of D-Trp was retained at almost zero. The adsorption selectivity of chirality in liposome membrane was further studied by investigating the adsorption of other amino acids. Similar tendency was observed in the case of other amino acids. In general, amino acids at D-form were not adsorbed on the DPPC liposome membrane, while those at L-form were adsorbed, depending on their type. Polar or charged amino acids (His, Asp, etc.) show the higher adsorption behavior. Based on the above findings, the optical resolution was performed through the equibrillium dialysis, equipped with the liposome immobilized hydrogel, by selecting the L-/D-Trp as target materials, resulting in the higher chiral selectivity.