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| Type |
Poster Presentation |
| Area |
Organic Chemistry |
| Room No. |
Event Hall |
| Time |
4월 19일 (목요일) 11:00~12:30 |
| Code |
ORGN.P-455 |
| Subject |
Synthesis of a Label-Free Föster Resonance Energy Transfer Probe for the Detection of p21-activated Kinase (PAK1) |
| Authors |
A Ro Han, Sang Jeon Chung1,*
Pharmacy, Sungkyunkwan University, Korea
1Department of Chemistry, SungKyunKwan University, Korea
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| Abstract |
Phosphatases and kinases play an important role in cellular signaling pathways where they are involved in the (de)phosphorylation of biomolecules. Dysregulation of protein (de)phosphorylation is associated with cell survival and can lead to numerous diseases (e.g., cancer, diabetes, and obesity) rendering phosphatases and kinases as viable drug targets for cancer treatment research. PAK1 is a member of the serine/threonine-protein kinase family, and plays a crucial role in the regulation of diverse cellular processes, e.g., metastasis, growth, and cell cycle progression. The implication of PAK1 in diverse cancers necessitates the development of a simple and robust detection assay. Conventional phosphorylase detection assays, e.g., the use of radioactive isotopes or ELISA, may require special facilities, are laborious and expensive. Here we report the development of a PAK1 specific fluorescence probe for the real-time detection of PAK1 using a label-free Föster Resonance Energy Transfer (FRET) approach. FRET involves radiation-less energy transfer between two suitable fluorophores when they are in proximity. Classically, FRET requires the labeling of (bio)molecules with both, an FRET donor and FRET acceptor. However, covalent modification of biomolecules may induce conformational and structural changes thereof. Our label-free FRET approach utilizes active site tryptophan residues of PAK1 as the FRET donor in conjunction with target specific probes equipped with a suitable FRET acceptor. Our probe is based on a known PAK1 inhibitor and is factionalized with a coumarin derivative, a known FRET acceptor to tryptophan. The developed FRET based PAK1 detection assay facilitates high throughput screening of potential drug candidates for the treatment of PAK1 related diseases. |
| E-mail |
we3978@daum.net |
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121st General Meeting of the KCS