Our research begins with the relationship between molecular structure and function. We combine organic synthesis with photophysical analysis and computation to develop molecules that help us observe and investigate biological systems. Our current focus on fluorescent probes and bioorthogonal chemistry provides a foundation for exploring new tools based on fluorophore–protein interactions. In the long term, we hope these molecular tools will contribute to disease diagnostics and the discovery of new bioactive molecules.
분자 구조가 성질과 기능을 어떻게 결정하는지 이해하면, 원하는 기능의 분자를 만들 수 있습니다. 유기합성, 광물리적 분석, 계산화학을 연결해 형광 프로브와 생물직교화학 분자도구를 개발하고, 새로운 형광분자와 단백질 간의 상호작용을 직접 설계합니다. 장기적으로는 이러한 분자 도구를 질병 진단과 새로운 생리활성 물질 발굴에 사용하고자 합니다.
How does molecular structure determine fluorescence? We investigate this relationship through organic synthesis, photophysical measurements, and DFT/TD-DFT calculations. Building on work with tunable fluorophore scaffolds, we aim to develop probes whose signals respond to their local environment or a specific molecular event. We are particularly interested in understanding the mechanisms behind these responses and using that knowledge to guide molecular design. Future applications include fluorescence lifetime imaging and the observation of multiple biological targets.
Keywords: Organic synthesis · Fluorescent probes · DFT/TD-DFT · Environment-sensitive probes · Fluorescent bioimaging
Bioorthogonal reactions allow us to label biomolecules selectively in complex biological environments. Our work on tetrazine-based probes examines how molecular structure and reaction partners influence fluorescence after a reaction. These insights support the design of probes for selective labeling and multicolor imaging. Building on this foundation, we aim to explore new reaction designs for chemical biology, including approaches to identify the protein targets of bioactive molecules and to investigate proteins in close proximity.
Keywords: Tetrazine chemistry · Fluorogenic probes · Bioorthogonal labeling · Multicolor imaging
Binding to a protein can change the environment and conformation of a fluorophore, altering its optical properties. We aim to understand and use these effects by combining fluroescent small-molecule design with protein structure prediction and AI-assisted binder design. This developing research direction explores complementary approaches: designing fluorophores that interact with proteins and designing proteins that bind selected fluorophores. Our long-term goal is to create fluorescent tools for monitoring protein states and protein–protein interactions.
Keywords: Protein–ligand interactions · Protein modeling · AI-assisted binder design · Fluorescent sensors
We welcome discussions on fluorescent probes, bioorthogonal labeling, and chemical biology tools for biological research.