|
|
| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Exhibition Hall 2+3 |
| Time |
10월 19일 (목요일) 11:00~12:30 |
| Code |
BIO.P-274 |
| Subject |
eDHFR and eDHFR_R12Y_Y100I proteins Inhibit Amyloid Fibril Formation of α-Synuclein |
| Authors |
So young Yoon, Lee Kyunghee*
Department of Chemistry, Sejong University, Korea
|
| Abstract |
Building on our previous work with FKBP-based system, we investigated regulator protein(s) for amyloid fibril formation of α-synuclein (αSyn). In the present study, E. coli dihydrofolate reductase (eDHFR) and its mutant (eDHFR_R12Y_Y100I) were cloned in pET28a vector to produce bacterial expression plasmids using PCR and site directed mutagenesis. Both eDHFR and eDHFR_DD (R21Y_Y100I as destabilization domain (DD)) was successfully expressed in BL21(DE3) in the presence of ITPG and purified by Ni2+-affinity chromatography. According to the thioflavin T (ThT) fluorescence assay, we observed that eHDFR inhibited the amyloid fibril formation of αSyn in a dose-dependent manner. It is noteworthy that the inhibitory effect of eDHFR_DD is more profound than that of eDHFR, suggesting an important role of DD as a regulator of amyloid fibril formation. |
| E-mail |
gee0528@gmail.com |
|
120th General Meeting of the KCS