Catalytic acyl transfer modification of nuclear receptors and detection by in-gel labeling
Author(s) | Guo, Ge | |
Date Accessioned | 2019-10-17T12:14:23Z | |
Date Available | 2019-10-17T12:14:23Z | |
Publication Date | 2016 | |
Abstract | Androgen receptor (AR) signaling plays a central role in prostate development and homeostasis as well as the progression of prostate cancer (PCa). Upon hormone binding, AR enters nucleus and induces down-stream expression of specific genes. Post-translational modification of AR could alter this signaling process and serve as an alternate approach in PCa treatment. ☐ In this study, we prepared N-acetylcysteamine (NAC) mimicking a charged CoA as an alkyne group substrate. As the structure of SAMT has been reported to act as an acyl transfer catalyst, we combined its structure with a ligand for AR and perform proximity-directed protein labeling to modify a lysine residue on AR. Efficiency and specificity of the labeling are evaluated with fluorogenic click reaction in vitro and in cell. The in-solution and in-gel detection limit are assessed, against small molecule reference and Bovine Serum Albumin (BSA) reference, respectively. ☐ Our result indicated that with the method discussed, the proximity-directed labeling has not been able to deliver a satisfactory efficiency and selectivity. The methods still show great potential and needs further diagnosis and optimization. | en_US |
Advisor | Koh, John T. | |
Degree | M.S. | |
Department | University of Delaware, Department of Chemistry and Biochemistry | |
Unique Identifier | 1123215449 | |
URL | http://udspace.udel.edu/handle/19716/24478 | |
Publisher | University of Delaware | en_US |
URI | https://search.proquest.com/docview/1853453070?accountid=10457 | |
Title | Catalytic acyl transfer modification of nuclear receptors and detection by in-gel labeling | en_US |
Type | Thesis | en_US |