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  • 02월 19일 10시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능
대회명 대한화학회 제121회 학술발표회 및 총회
등록일 2018년 2월 3일 16시 34분 33초
접수번호 3603
발표코드 BIO.O-6 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간 목 10시 : 40분
발표형식 구두발표
발표분야 Life Chemistry - Oral Presentation in Chemistry of Life
저자 및 공동저자 Kyeng Min Park
Center for Self-assembly and Complexity, Institute for Basic Science, Korea
제목 Ultrastable Synthetic Host-guest interactions: a Novel Supramolecular Tool for Chemical Biology
내용 The streptavidin (Sv)-biotin (BT) system with a high binding affinity (K ~ 1013 M-1) as a protein-ligand binding pair has been utilized as a powerful chemical biology tool for protein imaging, purification, and analysis. However, the Sv-BT pair has some intrinsic shortcomings; 1) interference of binding from endogenous biotins that are widespread in cells and tissues, and involved in various metabolic pathways in many species 2) false positive signals caused by endogenously biotinylated proteins 3) difficulty in chemical modification and instability of streptavidin (protein) degraded by proteases in cellular conditions. Recently, we developed a new ultrastable synthetic binding pair as “supramolecular latching system” consisting of cucurbit[7]uril (CB[7]) and ferrocenemethylamine (FcA) or adamantineamine (AdA), which has almost comparable (or even higher) binding affinity (K ~1012-15 M-1) to Sv-BT with unique features including 1) bio-orthogonality in binding which is not affected by endogenous biomolecules such as biotin, 2) a small size with stable and robust chemical structure, 3) scalability using known chemical synthetic methods and 4) convenient uses with easy-to-handle and 5) controllable binding affinity by treating strong competitors, by which the binding of the synthetic host-guest pair can be modulated on-demand as supramolecular latch “on” and “off”. Here, I will talk about our recent efforts to utilize this supramolecular latching system for visualization of spatially specific proteins in and on living organisms such as cells and Caenorhabditis elegans (C. elegans). In addition, our extended efforts to utilize it for spatiotemporal proteome mapping in living cells by combining with a promiscuous protein labeling method will be introduced.
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