(2019-Current) Chief Scientist(2017-2019) Lead Scientist(2014-2017) Sr. Scientist(2011-2014) Scientist(2009-2011) Associate Scientist-Lead an interdisciplinary team comprising chemists, biologists, and biochemists at iProgen, overseeing the development of our protein delivery technology.-Spearheaded the design and execution of innovative strategies to advance intracellular protein delivery technology.-Co-inventor to all of iProgen's patented technologies to date.-Responsible for producing scientific content for patents and publications, as well as resolving technololgical issues and challenges.-Collaborates closely with management to establish and execute academic and industry partnerships aimed at unlocking new therapeutic possibilities through iProgen's extensive range of protein delivery technologies.Lee, K.H., Lin L.Y., Vaidyanathan R., Lario P. "Antibody-Payload Conjugates with Enhanced Delivery Domain and Uses Thereof" Publication No.: WO/2021/092672Lee, K.H., Lin L.Y., Want A. (2015) "Intracellular Protein Delivery" Publication No.: US 2015/0191710 A1Pastushok et al., (2019) A Novel Cell-Penetrating Antibody Fragment Inhibits the DNA Repair Protein RAD51. Sci. Rep., 9, 11227, PubMedID: 31375703

- Formulated production strategies for the manufacturing of cell-permeable antifreeze proteins.- Provides scientific leadership, expertise, and guidance in the design, production, assessment, and utilization of cell-permeable antifreeze proteins.- Addresses and resolves technical challenges faced by the scientific team.- Supervises the drafting of patents and publications, as well as the training of essential scientific personnel.

- Structural biology of membrane proteins involved in human bacterial pathogenesis- Engineered 46 truncation mutants of enzymes involved in teichoic acid biosynthesis. Assisted in developing purifications of membrane-associated teichoic acid polymerases; - Assisted in growing protein crystals at 4 degree C (i.e., refrigerated room), and solved the high-resolution crystal structures of lipooligosaccharide sialyltransferase. Modeled substrates into the crystal structure of sialyltransferase. Designed and cloned 22 single point mutants of sialyltransferase. Collaborated with medicinal chemists, and characterized the enzyme kinetics of mutants.- Assisted a colleague in growing protein crystals under oxygen-free condition (i.e., Nitrogen gas-filled glove box), and solved the protein structures. Lin et al., (2011) Structure and mechanism of the lipooligosaccharide sialyltransferase from Neisseria meningitidis. J. Biol. Chem., 286, 37237-37248, PubMedID: 21880735. Lovering et al., (2010) Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis. Nat. Struct. Mol. Biol., 17, 582-589, PubMedID: 20400947.Dresen et al., (2010) A falvin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolism. J. Biol. Chem., 285, 22264-22275, PubMedID: 20448045.

- Enzymology and engineering of bioluminescence marker – bacterial luciferase - Collaborated with computational chemists and modeled luciferase-substrate complexes. The modeled strcuture was verified correct and validated by X-ray crystallographic method in 2009 by Campbell et al. (2009) Biochemistry, 48, 6085-6094, PubMedID: 19435287.- Mastered the techniques involved in BioRad M13 in vitro site-directed mutagenesis. Designed and cloned 77 site-specific point mutants of bacterial luciferase; Engineered the luciferases with altered light emission spectra. Characterized the enzyme kinetics of luciferase mutants; Trained 6 undergraduate students as laboratory assistants.Lin et al., (2004) “Changes in the kinetics and emission spectrum on mutation of the chromophore-binding platform in Vibrio harveyi luciferase” Biochemistry 43: 3183-3194 [PMID: 15023068]Lin et al., (2002) “Implications of the reactive thiol and the proximal non-proline cis-peptide bond in the structure and function of Vibrio harveyi luciferase” Biochemistry 41: 9938-9945 [PMID: 12146958]Lin et al., (2001) “Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data” Protein Sci. 10: 1563-1571 [PMID: 11468353]

Molecular modeling of protein-ligand complex structure- Developed a strategy for modeling substrates in the crystal structure of bacterial luciferase. The modeled strcuture was verified correct and validated by X-ray crystallographic method in 2009 by Campbell et al. (2009) Biochemistry, 48, 6085-6094, PubMedID: 19435287.Lin et al., (2001) “Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data” Protein Sci. 10: 1563-1571 [PMID: 11468353]

Department of Biochemistry