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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Exhibition Hall 2+3 |
| Time |
10월 19일 (목요일) 11:00~12:30 |
| Code |
BIO.P-261 |
| Subject |
Ultrastable Synthetic Host-Guest Interaction Based Supramolecular Latching System as a Versatile Bioimaging Tool in Chemical Biology [우수포스터상] |
| Authors |
KyungLock Kim, Gihyun Sung1, Meng Li2, ARA LEE3, Kyeng Min Park4,*, Kimoon Kim5,*
Bernstein Laboratory, Massachusetts General Hospital and Harvard Medical School, United States
1AMS, Pohang University of Science and Technology, Korea
2Center for Self-Assembly and Complexity, Institute for Basic Science, China
3Advanced Materials Science, POSTECH, Korea
4Center for Self-assembly and Complexity, Institute for Basic Science, Korea
5Department of Chemistry, Pohang University of Science and Technology, Korea
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| Abstract |
Protein-ligand binding pairs such as streptavidin-biotin (SA-BT) have been used as an efficient tool for fluorescence-based cellular imaging to examine the function, structure and localization of proteins of interest. However, the SA-BT based methods suffer from intrinsic drawbacks including their large size, interference of endogenous biotinylated protein and enzymatic degradations. Herein, we demonstrate that the supramolecular latching system based on the ultrastable synthetic host-guest molecules, cucurbit[7]uril (CB[7]) and adamantyl (AdA) or ferrocenyl ammonium (FcA), can be exploited for location-specific protein visualization by employing a variety of different conjugation methods.1 Proteins of interest were labeled with AdA by using location-specific labeling methods and selectively visualized upon treatment of cyanine 3-conjugated CB[7] (Cy3-CB[7]),2 with no interference from endogenous biomolecules, which enables us to generate clear fluorescence images for accurate and precise protein analysis using fluorescence microscopy. This ultrastable synthetic binding pair system using CB[7] can be a new tool for cell imaging. Additionally, this newly developed synthetic system can be used with conventional SA-BT based systems, which may enable us to visualize proteins, with high resolution, involved in various biological processes such as protein-protein interactions and organelle communications.
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| E-mail |
ghsung@postech.ac.kr |
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120th General Meeting of the KCS