Lab Introduction & Major Research Interests
We are interested in the genes and proteins associated with the pathogenic pathway of Alzheimer’s disease (AD), especially the ones involved in the production of amyloid beta (Abeta) peptide. Specifically, we are studying the interactions among those macromolecules using the approaches of enzymology, molecular biology, and bioinformatics. The ultimate goal is to develop potential therapeutic agents that will retard or even halt the development of AD by slowing down the accumulation of Abeta.
current working hypothesis
Recent Representative Publication ( * corresponding author)
1. A newly designed molecule J2326 for Alzheimer’s disease disaggregates amyloid fibrils and induces neurite outgrowth, P.-T. Chang, R.S. Talekar, F.-L. Kung, T.-R. Chern, C.-W. Huang, Q.-Q. Ye, M.-Y. Yang, C.-W. Yu, R.R. Deore, S.-Y. Lai, J.-H. Lin, C.-S. Chen, G. S. Chen, J.-W. Chern (2015) Neuropharmacol. 92:146-157.
2. FKBP12 regulates the localization and processing of amyloid precursor protein in human cell lines, F.-L. Liu, T.-Y. Liu, F.-L. Kung (2014) J. Biosci. 39(1):85-95.
3. An improved screening model to identify inhibitors targeting zinc-enhanced amyloid aggregation, P.-T. Chang, F.-L. Kung, R. S. Talekar, C.-S. Chen, S.-Y. Lai, H.-Y. Lee, J.-W. Chern (2009) Anal. Chem. 81(16):6944-6951.
4. The intracellular domain of amyloid precursor protein interacts with FKBP12, F.-L. Liu, P.-H. Liu, H.-W. Shao, and F.-L. Kung (2006) Biochem. Bioph. Res. Co. 350(2):472-477.
5. The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein, T.-Y. Chen, P.-H. Liu, C.-T. Ruan, L. Chiu, F.-L. Kung (2006) Biochem. Bioph. Res. Co. 342(1):266-272.