Ping Li, Ph.D.
University Outstanding Scholar, Associate Professor, and Director of Protein and Biopolymer Analysis Core Lab (PBACL)
Contact information
Office: 61 Chalmers Hall
Email: pli@ksu.edu
Education
Ph.D. Duke University, 2005
Postdoc, Massachusetts Institute of Technology, 2006-2011
Areas of Specialty
- Polyhydroxyalkanoate (PHA) biosynthesis, regulation, and utilization
- Bacterial enzymes involved in lignin degradation
- Protein methyltransferases in epigenetics
Research
Using enzymology, synthetic organic chemistry, and molecular biology as major tools to study and manipulate biologically important enzymes/proteins. Currently, I have three projects in my lab.
Polyhydroxyalkanoate (PHA) biosynthesis, regulation, and utilization
PHAs are carbon storage polymers produced by a variety of bacteria under conditions that limit nutrients except for carbon. The environmentally friendly PHA bioplastics are considered as an ideal alternative to petroleum-derived plastics that are non-biodegradable. Our goal is to understand PHA homeostasis at the molecular level such that metabolic- and protein-engineering in bacteria can be performed to produce PHA polymers economically. Moreover, study of PHA production can serve as a paradigm to understand widespread template-independent polymerizations where the mechanism remains enigmatic.
Bacterial enzymes involved in lignin degradation
Lignin is a recalcitrant polymer consisting of various phenylpropane-based monomers linked together by C-C and C-O-C bonds, which is the most abundant renewable carbon source on earth next to cellulose. The cost of lignin degradation has been a major indicator for the competitiveness of biofuels vs. petroleum-based gasoline. It is well known that fungus contains a series of redox metalloenzymes that can efficiently degrade lignin. However, until now they have not been used at industrial scales due to difficulties in modulation of fungal genetics and production of fungal proteins. Therefore, there is a paradigm shift to seek for bacterial enzymes for lignin degradation. Our goal is to identify and develop them into a system that can be used to process lignin degradation economically at large scales.
Protein methyltransferases in epigenetics
Methylation is one of commonly observed protein posttranslational modifications that play important roles in signaling network and epigenetic regulation. Defects in the methylation have been linked to various diseases including cancers, neurological disorders, and abnormalities in development. Aside from protein lysine and arginine methyltransferases, a new type of protein methyltransferases, α-N-terminal RCC1 methyltransferases (NRMTs), was recently discovered in eukaryotes and human. Limited study of NRMTs suggests that they may be linked to cancers. Our goal is to identify the processes and/or targets involving NRMT for potential cancer therapy.
Selected Publications
Suzauddula, M., Avalos-Calleros, J.A., Khadka, S., Li, P., Park, S., Wang, D., Sun, X.S., Wang, W. Anthocyanin-enriched bioengineered tomato suppresses PI3K/Ras signaling and induces cell cycle arrest and apoptosis in human SW480 colon cancer cells. Under review.
Habarakadage, B., Rajendran, S., An, C., Khadka, S., Anderson, M.J., Koehne, J., Hua, D.H., Li, P., Li, J. Peptide substrate optimization for multiplex protease activity profiling under neutral pH conditions using Au microelectrode arrays. Under review.
Silva, V.D., Tran, A., Wu, W., Averkiev, B.B., Li, P., Guidez, E.B., Aakeroy, C.B. From tunable chalcogen bonding to enhanced chemotherapeutic properties. Cryst. Growth Des. 2025, 25, 6075, DOI: 10.1021/acs.cgd.5c00529.
Duan, H., Wu, W., Li, P., Bouyain, S., Garcia, B.L., Geisbrecht, B.V. Blocking Activation of the C1r Zymogen Defines a Novel Mode of Complement Inhibition. J. Biol. Chem. 2025, 301, 108301, DOI: 10.1016/j.jbc.2025.108301.
Cui, M., Wu, W., Li, Q., Qi, G., Liu, X., Bai, J., Chen, M., Li, P., Sun X.S. Unlocking the potential of human-induced pluripotent stem cells: Cellular responses and secretome profiles in peptide hydrogel 3D culture. Cells 2024, 13: 143. DOI: 10.3390/cells13020143.
Xu, X., Herdendorf, T.J., Duan, H., Rohlik, D.L., Roy, S., Zhou, H., Alkhateeb, H., Khandelwal, S., Zhou, Q., Li, P., Arepally, G.M., Walker, J.K., Garcia, B.L., Geisbrecht, B.V. Inhibition of the C1s protease and the classical complement pathway by 6-(4-phenylpiperazin-1-yl)pyridine-3-carboximidamide and chemical analogs. J. Immunol. 2024, 212, 689-701, DOI: 10.4049/jimmunol.2300630.
Zhou, Q., Wu, W., Jia, K., Qi, G., Sun, X.S., Li, P.* Design and characterization of PROTAC degraders specific to protein N-terminal methyltransferase 1. Eur. J. Med. Chem. 2022, 244: 114830, DOI: 10.1016/j.ejmech.2022.114830.
Li, Q., Qi, G., Lutter, D., Beard, W., Souza, C.R., Highland, M.A., Wu, W., Li, P., Zhang, Y., Atala, A., Sun, X.S. Injectable peptide hydrogel encapsulation of mesenchymal stem cells improved viability, stemness, anti-inflammatory effects, and early stage wound healing. Biomolecules 2022, 12: 1317, DOI: 10.3390/biom12091317.
Pradyawong, S., Shrestha, R., Li, P., Sun, X.S., and Wang, D. Effect of pH and pH-shifting on lignin–protein interaction and properties of lignin-protein polymers. J. Polym. Environ. 2022, 30, 1908-1919, DOI: 10.1007/s10924-021-02319-8.
Shrestha, R., Jia K., Khadka S., Eltis L.D., and Li P.* Mechanistic insights into DyPB from Rhodococcus jostii RHA1 via kinetic characterization, ACS Catal. 2021, 11, 5486-5495, DOI: 10.1021/cascatal.1c00703.
Jia, K., Huang, G., Wu, W., Shrestha, R., Wu, B., Xiong, Y., and Li, P.* In vivo methylation of OLA1 revealed by activity-based target profiling of NTMT1, Chem. Sci. 2019, 10, 8094-8099, DOI: 10.1039/C9SC02550B.
*Highlighted as a back-cover article .