일시 : 2017년 3월 29일(수) 오후5시-7시

장소 : 과학관 604호

연사 : 정상전 교수님(동국대, 화학과)

We have developed an intrinsic fluorescence resonance energy transfer (iFRET) technology, which can detect a native target protein. The iFRET utilizes tryptophan residues of the target protein and a cell-permeable target-specific probe, which is selectively excited by the intrinsic tryptophan fluorescence (λem = 350 nm), as FRET donors and acceptors, respectively. As the Förster distance between the tryptophan residues and the iFRET probe is about 2 nm, an iFRET signal is generated by specific interaction of the target protein and the selective iFIT probe with a very low chance of signal generation from a nonspecific binding. Using iFRET, we have detected various proteins without any modification. Based on the iFRET, we have also developed an

intrinsic fluorescence resonance energy transfer (iFRET) imaging technique (iFIT) to detect a native target protein and its interaction with drugs in live cells. The iFIT employs a deep UV biological microscope in combination with a target-specific fluorescent probe. A deep UV biological microscope equipped with a quartz objective and two optical filters (288 and 365 nm) on a shutter was constructed to facilitate the detection of the iFRET signal upon binding of the probe to its target, in live cells. We successfully achieved imaging of native streptavidin in live cells with the thus developed iFIT, after simple treatment of live cells with the corresponding iFIT probes.