|
Type |
Poster Presentation |
Area |
Analytical Chemistry |
Room No. |
Event Hall |
Time |
4월 19일 (목요일) 11:00~12:30 |
Code |
ANAL.P-292 |
Subject |
Characterization study for partial active site structure of microcystin using 2D-NMR |
Authors |
Nayoung Lee, JungEun Kim, GilHoon Kim, Hoshik Won1,* Department of Applied Chemistry, Hanyang University, Korea 1Department of Chemical and Molecular Engineering, Hanyang University, Korea |
Abstract |
The microcystin is a cyclic heptapeptide from metabolites of cyanobacteria. It is a potent inhibitor of the catalytic subunits of protein phosphatase-1 and –2A (PP-1c and PP-2Ac) as well as powerful tumor promoter.
The active site of microcystin actually has two metal ions Fe2+/Zn2+ close to the nucleophilic portion of PP-1-microcystin complex and various monovalent/divalent ion binding studies were made for microcystin and protein phosphatase-1-microcystin complex.
Recently reported that, metal ions in the protein phosphatase create a region of positive electrostatic potential at the active site and potassium salt inhibits growth of cyanobacteria.
To investigate the detail structure information elucidating and catalytic roles of metal ions in microcystin, we prepared two synthesized mimic peptides micro-A and micro-B which has similar structure to microcystin active site.
The solution structure determination of two peptides were assigned with 1H-NMR and 2D-NMR (COSY, TOCSY, NOESY) experiments. On the basis of these completely assigned NMR spectra and distance data, distance geometry(DG) and molecular dynamic(MD) were carried out to determine the structures of micro-A and micro-B. The proposed structure was selected by comparisons between experimental NOE spectra and back-calculated 2D-NOE results from determined structure showing acceptable agreement. |
E-mail |
kghpotter@naver.com |
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