Earticle

초록

영어

Protein kinases play a key role in numerous cellular functions and have been the targets for investigation of specific signaling pathways as well as for development of therapeutic drugs. Rapid and simple analysis of kinases activity, therefore, is prerequisite for understanding various physiological and pharmacological functions of the kinases. Here we demonstrate a rapid and simple method to detect the phosphorylation of peptide substrates by using the fluorescence resonance energy transfer (FRET) between quantum dot (QD) as a donor and the dye-tethered peptide as an acceptor. Compared to a nonphosphorylated peptide, a synthetic phosphorylated one was strongly attached on the surface of the carboxyl QD in the presence of ZnCl2, due to a metal-coordination effect, thus leading to higher energy transfer efficiency. Metal ion-free condition and other divalent ions (CoCl2, ZnCl2, and FeCl2) did not give rise to the change in the energy transfer. Upon kinase reaction, the energy transfer efficiency between the QD and the peptide substrate was modulated. Based on these observations, we anticipate that our developed method will have a great potential for analyzing protein kinase activity with high sensitivity and thus will be useful for real-time monitoring.

키워드

저자

• Ji-In PARK [ Dept. of Life Science, Hanyang University, Seoul, 133-791. ]
• Bu Taek LIM [ Dept. of Life Science, Hanyang University, Seoul, 133-791. ]
• Hye Rim HONG [ Dept. of Life Science, Hanyang University, Seoul, 133-791. ]
• Geum Nae NAM [ Dept. of Life Science, Hanyang University, Seoul, 133-791. ]
• Young-Pil KIM [ Dept. of Life Science, Hanyang University, Seoul, 133-791. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576