Tel: (05)2720411 ext. Office 66511 Lab 61523

 Fax: (05)2722871

 Email: biocil@ccu.edu.tw

• 1999 - 2005 Ph. D., Biophysical Chemistry, Yale University, USA
• 1996 - 1998 M. S., Chemistry, National Tsing Hua University, Taiwan
• 1992 - 1996 B. S., Chemistry, National Tsing Hua University, Taiwan

• 生物化學
• 生物物理
• 生物無機化學
• 生物奈米影像

• 2019- Present Professor,Department of Biomedical Sciences, National Chung-Cheng University, Chia-Yi, Taiwan.

• 2005 - 2007 Post-Doctoral Associate, Medical Biotechnology Center, University of Maryland Biotechnology Institute, USA  博士後研究員 美國馬禮蘭大學生物技術研究所
• 1998 - 1999 研究助理 中央研究院化學所

Biochemical and biophysical studies on misfolding of prion proteins.
Nanoimaging of prion fibrils.

Prion diseases are progressive neurodegenerative disorders that affect both humans and animals, such as Creutzfeldt-Jakob disease (CJD) in humans, bovine spongiform encephalopathy (mad cow disease) in cows and Scrapie in sheep. Up to date, there is no therapeutic treatment to control or to cure prion diseases. Prion diseases are caused by accumulation of prion amyloid fibrils resulted from misfolding of normal α-helix rich prion proteins into β-sheet rich prion proteins. How prion monomers misfold and convert to fibrils is not know yet. We are interested in studying the mechanism of the prion fibril formation by molecular spectroscopy and nanoimaging.

Distinguish National Science Council (Taiwan) undergraduate research (1996)

1. Cheng-I Lee, Nai-yuan Chang, “Characterizing the denatured state of human prion 121-230.”Biophysical Chemistry  (2010) 151, 86-90, [SCI], (NSC 98-2113-M-194-0003).
2. Ying Sun, Natallia Makarava, Cheng-I Lee, Pongpan Laksanalamai, Frank T. Robb, Ilia V. Baskakov, “Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size.” Journal of Molecular Biology.  (2008) 376, 1155-1167 [SCI].
3. Natallia Makarava, Cheng-I Lee, Valeriy G. Ostapchenko, Ilia V. Baskakov, “Highly promiscuous nature of prion polymerization,” Journal of Biological Chemistry  (2007) 282, 36704-36713 [SCI].
4. Cheng-I Lee, Qingyuan Yang, Veronique Perrier, Ilia V. Baskakov, “The dominant negative effect of the Q218K variant of the prion protein does not require protein X , ”Protein Science  (2007) 16, 2166-2173 [SCI].
5. Cheng-I Lee, K. V. Lakshmi, Gary W. Brudvig, “Probing the functional role of Ca2+ in the oxygen-evolving complex of Photosystem II by metal ion inhibition, ”Biochemistry  (2007) 46, 3211-3223 [SCI].
6. Leonid Breydo, Ying Sun, Natallia Makarava, Cheng-I Lee, Vera Novitskaia, Olga Bocharova, Joseph P. Y. Kao, Ilia, V. Baskakov, “Nonpolar substitution at the C-terminus of the prion protein, a mimic of the glycosylphosphatidulinositol anchor, partially impairs amyloid fibril formation, ”Biochemistry  (2007) 46, 852-61 [SCI].
7. Cheng-I Lee, Gary W. Brudvig, “Investigation of the functional role of Ca2+ in the oxygen-evolving complex of Photosystem II: a pH-dependence study of the substitution of Ca2+ by Sr2+”, Journal of the Chinese Chemical Society  (2004) 51, 1221-1228 [SCI].
8. Sergei Vassiliev, Cheng-I Lee, Gary W. Brudvig, Doug Bruce, “Structure-based kinetic modeling of excited-state transfer and trapping in histidine-tagged Photosystem II core complexes from Synechocystis”, Biochemistry  (2002) 41, 12236-12243 [SCI].
9. Cheng-I Lee, Yuan-Pern Lee, Xuefeng Wang, Qi-Zong Qin, “Isomers of N2O3: Observation of trans-cis N2O3 in solid Ar”, Journal of Chemical Physics  (1998) 109, 10446-10455 [SCI].
10. Li-Shiun Chen, Cheng-I Lee, Yuan-Pern Lee, “Isomers of SO2: Infrared absorption of SOO in solid argon”, Journal of Chemical Physics, (1996) 105, 9454-9460 [SCI].
11. 江素玉、李政怡、馮學深、蔡宛霖、羅祥文, “同步輻射圓二色光譜實驗站與應用” 科儀新知 (2009), 30(5), 9-17.