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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-259 |
| Subject |
Development of a new method for finding protease substrates and its application to study the protein degradation |
| Authors |
Ga-eul Eom, Seokhee Kim1,*
Chemistry, Seoul National University, Korea
1Division of Chemistry, Seoul National University, Korea
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| Abstract |
Proteases are one of the largest group of enzymes. Their deregulation is associated with pathogenesis of many human diseases due to the critical function of proteases in cellular processes, including protein quality control by degrading unfolded or misfolded proteins. The tools for searching the general protease substrate(s) are limited. So the development of a method that allow identification of general protease substrate(s) is a challenge of high interest, since it will not only enhance our understanding of the cellular functions of proteases, but will allow identification of targets for development of novel therapeutics.
In the system developed in our laboratory, proteases that have serine, cysteine and threonine residues in the active sites form an acyl-enzyme intermediate in the first step by combining with the substrate N-term fragment. Then, intermediates are hydrolyzed to complete cleavage in a general reaction. In the second step, if there are more of better nucleophiles than H₂O , they will form covalently-linked products with the substrate N-terminal fragment. These peptides are selected and sequenced by LC-MS/MS. Through this method, we will be able to identify the original substrate. This new method to profile substrate is named Trapping Proteolysis Intermediates (TraPI).
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| E-mail |
autumn1023@snu.ac.kr |
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120th General Meeting of the KCS