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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Highly sensitive membrane biosensor amplified by electrophoretic accumulation of membrane components

2008년 8월 12일 11시 59분 21초
36P263포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
금 <발표Ⅳ>
저자 및
이영광, 남좌민1
서울대학교 화학과, Korea
1서울대학교 화학부, Korea
A number of significant biochemical events such as intercellular signaling, immune response and viral infection which engage specific receptor-ligand interactions take place on the cell membrane surface, resulting in spatial reorganization of receptor-ligand complexes and then altering lateral mobility of membrane lipids. Recently, several attempts to employ the alterations in structural arrangement of receptor-ligand architecture and membrane fluidity as a signal in membrane biosensor have been made to probe membrane surface-related biological reactions at molecular level. Multivalent cholera toxin binding to the pentasaccharaide headgroup of membrane-incorporated GM1 lipids nucleates nanometer scale gel phase domains that extend beyond the immediate binding region. As a result, lipid phase state and chain organization change, affecting long-range lateral mobility of the major lipids that do not participate in the receptor-ligand binding events. We demonstrated that the membrane biosensor we proposed probes binding of a soluble protein to a membrane receptor using self-assembled lipid bilayer on silica surface, so-called supported lipid bilayer, as a sensing platform for systematic and controlled investigation. The difference in lipid mobility originating from cholera toxin binding events was amplified and visualized by electrophoretic accumulation of fluorophore-labeled lipid molecules within the confined region at near phase transition temperature of major lipids.