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陳佩燁 博士
副研究員
中央研究院生物化學研究所 504室
臺北市南港區115研究院路二段128號
TEL: +886-2-27855696 ext. 5040
FAX: +886-2-2788-9759
pyc@gate.sinica.edu.tw
陳佩燁的個人網站


My research interest is regarding protein folding and misfolding behaviors in order to answer how proteins can fold into its native structure and how certain proteins can misfold and cause disease. Studies about protein folding are mainly the development of new methodologies to explore the folding process in order to unravel the intrinsic folding properties. Studies about protein misfolding are focus on two diseases: prion disease and Alzheimer’s disease. We are interested in studying the mechanism of amyloid fibril formation, factors influencing molecular assembly, designing inhibitor for amyloid formation, and species barrier in prion disease.

1993,09 - 1998,04 博士, 生化系, 英國劍橋大學
1989,09 - 1991,06 碩士, 生化科學所, 國立臺灣大學
1985,10 - 1989,06 學士, 農業化學系, 國立臺灣大學

2010,05 - present 副研究員, 中央研究院生化所
2003,04 - 2010,05 助研究員, 中央研究院生化所
1999,06 - 2003,03 博士後研究員, 中央研究院化學所
1992,08 - 1993,07 研究助理, 中央研究院生物化學所

    論文列表
Revealing structural changes of prion protein during conversion from alpha-helical monomer to beta-oligomers by means of ESR and nanochannel encapsulation.
Yang, C., Lo, W. L., Kuo, Y. H., Sang, J. C., Lee, C. Y., Chiang, Y. W. & Chen, R. P. ACS Chem Biol (2015)
Thioflavin T and its photo-irradiative derivatives: Exploring their spectroscopic properties in the absence and presence of amyloid fibrils.
Hsu, J. C., Chen, H. L., Snoeberger, R. C., Luh, F. Y., Lim, T. S., Hsu, C. & Chen, R. P. J Phys Chem B (2013)
Observation of protein folding/unfolding dynamics of ubiquitin trapped in agarose gel by single-molecule FRET.
Yang, L. L., Kao, M. W., Chen, H. L., Lim, T. S., Fann, W. & Chen, R. P. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS (2012)
Slow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein.
Sang, J. C., Lee, C. Y., Luh, F. Y., Huang, Y. W., Chiang, Y. W. & Chen, R. P. Prion (2012)
Leu-138 in the bovine prion peptide fibrils is involved in the seeding discrimination related to codon-129 M/V polymorphism in the prion peptide seeding experiment.
Liao TY, Lee LY, Chen RP FEBS journal (2011)
A highly sensitive peptide substrate for detecting two Abeta-degrading enzymes: Neprilysin and insulin-degrading enzyme.
Chen PT, Liao TY, Hu CJ, Wu ST, Wang SS, Chen RP Journal of neuroscience methods (2010)
A new amyloid-like beta-aggregate with amyloid characteristics, except fibril morphology.
Chang ES, Liao TY, Lim TS, Fann W, Chen RP JOURNAL OF MOLECULAR BIOLOGY (2009)
Quantifying the Sequence-Dependent Species Barrier between Hamster and Mouse Prions.
Lee, L.Y., and Chen, R.P. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2007)
Measuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale.
Chen, R.P., Huang, J.J., Chen, H.L., Jan, H., Velusamy, M., Lee, C.T., Fann, W.S., Larsen, R.W., and Chan, S.I. Proc. Natl. Acad. Sci. USA (2004)
One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide.
Chen, P.Y., Lin, C.C., Chang, Y.T., Lin, S.C., and Chan, S.I. Proc. Natl. Acad. Sci. USA (2002)

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