Research Interest: Analytical Probe and Protein Biotechnology (a branch of chemical biology) Based on physicochemical principle for interactions of proteins with their ligands, chemometrics is utilized to mine information associated with the forces of their interactions, the strength for their bioaffinity interactions (affinities), the quantities of counterpart biomolecules, which facilitates the development of methods and probes for in vitro diagnostics and drug screening, protein ligands and protein mutants of biological significance. In detail, our research interest covers the following topics:

(1) New methods and probes for in vitro diagnostics and drug screening: to enhance analytical efficiency and precision, probes are designed based on mechanistic ways of bioaffinity interactions and new process to mine information are developed; such new methods and probes are applied to simultaneous assays of multiple components in single channel, especially for simultaneous immunoassays of multiple components in single channel, the screening of ligand mixtures, the screening of enzyme mutants, homogenous bioaffinity assay with tryptophan residues as resonance-energy-transfer donors, and linear response by competitive bioaffinity assay;

(2) With PDE and GST as examples, methods are developed to rational and combinatorial design of isozyme-selective inhibitors, pro-inhibitors and soft inhibitors, the screening of such inhibitors, and the potential as therapeutic agents;

(3) With uricase, arylsulfatase and alkaline phosphatase as examples, rational design and directed evolution of enzymes are studied, together with high-throughput screening and evaluation of their mutants, chemical modification of proteins; rational design of fused proteins as therapeutic agents;

(4) Affinity-labeling and site-specific immobilization of protein targets, the cross-linking/conjugation of enzymes and antibodies.