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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Exhibition Hall 2 |
| Time |
4월 19일 (금요일) 11:00~12:30 |
| Code |
LIFE.P-343 |
| Subject |
Methodology Development of Screening Weak Binders by Using NMR Spectroscopy |
| Authors |
Yoonjin Um, Young Kee Chae*
Department of Chemistry, Sejong University, Korea
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| Abstract |
We have been developing a novel screening approach by using NMR spectroscopy. Our method is based on the hypothesis that any molecule that binds to a very large target protein will lose its NMR signal due to a very slow tumbling rate, which is a fundamental phenomenon of NMR spectroscopy. Our goal is to screen as many molecules as possible in a super high throughput fashion. After finding weak binders, the next move will be to combine those molecules to make stronger binders that can then be applied pharmaceutically. Our approach to make a very large target protein is through the formation of the supramolecular complex by using a polypeptide (ELP) that tends to aggregate, not get denatured, at slightly elevated temperatures. To prove our hypothesis, we chose 2 proteins as testable targets: the maltose binding protein (MBP) and glutathione S-transferase (GST). We fused those two proteins to an ELP. To prepare a ligand pool that can be screened by using a simple NMR technique, we labeled the candidate molecules with C-13 by feeding E. coli or yeast with C-13 glucose as a sole carbon source. Our preliminary data shows that MBP picked up one compound whose signal disappeared as we expected, and we are now in the process of identifying it. We hope this new approach will provide an alternative way to design suitable compounds from a pool of weak binders. This work has been supported by Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (NRF-2017R1D1A1A02017545). |
| E-mail |
ykchae@sejong.ac.kr |
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123rd General Meeting of the KCS