Over the past decade, sulfur ylides have emerged as versatile tools in nucleophilic addition, rearrangement, and annulation chemistry, with significant advances reported. Their compatibility with mild, metal-free conditions and broad functional-group tolerance further enhances their value in contemporary synthesis. Beyond their classical role as sulfur ylides, sulfonium ions can engage in diverse activation modes, including single-electron transfer (SET) processes leading to homolytic C–S bond cleavage and carbon-centered radical reactivity, transition-metal-mediated oxidative addition into the C–S bond to form organometallic intermediates for cross-coupling, and photocatalyst-enabled activation to generate ylide-derived radicals capable of mediating hydrogen atom transfer (HAT). Our group focuses on the application of sulfonium ions in synthetic methodology development.

Diabetes mellitus is a major global health challenge, with type 2 diabetes mellitus (T2DM) accounting for over 90% of cases. A key pathological feature of T2DM is the aggregation of human islet amyloid polypeptide (IAPP, or amylin), an intrinsically disordered peptide co-secreted with insulin by pancreatic β-cells. The accumulation of IAPP amyloid deposits in pancreatic islets is closely associated with β-cell dysfunction and loss, leading to impaired insulin secretion and hyperglycemia. However, the mechanisms governing IAPP behavior and aggregation remain incompletely understood. Our group is eager to develop fluorescent probes capable of detecting IAPP fibril aggregation and monitoring its aggregation process in real time, thereby enabling deeper insight into the behavior of IAPP and its role in T2DM pathogenesis.

Human serum albumin (HSA), the most abundant protein in blood plasma, plays a pivotal role as a transport protein for both endogenous metabolites and exogenous drugs, making it essential for understanding drug pharmacokinetics. Among the available analytical approaches, fluorescent probe technology has emerged as a powerful tool for elucidating the binding sites and binding characteristics of drug–HSA interactions. However, most reported fluorescent probes bind exclusively to either subdomain IIA or subdomain IIIA of HSA, which significantly limits their broader applicability. To address this limitation, our group focuses on the development of fluorescent probes that selectively target specific HSA binding sites outside subdomains IIA and IIIA, thereby expanding their utility. In addition, by exploiting HSA’s intrinsic function as a carrier protein, we are dedicated to the development of near-infrared II (NIR-II) fluorescent probes that utilize HSA as a delivery vehicle to enhance bioavailability and enable effective in vivo imaging.

The development of artificial enzymes has attracted considerable interest because they can overcome the inherent limitations of natural enzymes and extend enzymatic functions to non-physiological conditions. As alternatives, nanomaterials offer advantages such as low cost, high stability, and robustness, enabling multiple enzyme-like activities. To date, various inorganic nanomaterials have been shown to catalyze the oxidation of diverse substrates in the absence of hydrogen peroxide (H₂O₂), exhibiting so-called oxidase-like activity, and such nanozymes have been applied in biological systems. However, the intrinsic oxidase-like activity of most nanozymes typically originates from transition or heavy metals, which severely limits their practical applications due to toxicity concerns. To address this issue, visible-light-activated small-molecule oxidase mimics have recently been developed as metal-free alternatives. In our group, we focus on the design and synthesis of photoactivated molecular-rotor-based oxidase mimics and their applications across diverse fields.