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.
2.2 Å Cryo-EM Tetra-Protofilament Structure of the Hamster Prion 108–144 Fibril Reveals an Ordered Water Channel in the Center.
Chen EH, Kao HW, Lee CH, Huang JYC, Wu KP*, Chen RP*
Journal of the American Chemical Society (2022)
Biodistribution analysis of an intranasal-delivered peptide by the nanoSPECT/CT imaging.
Lo WL, Wang YH, Chen EH, Wang SM, Chen LC, Chen RP*
Journal of Drug Delivery Science and Technology (2022)
Location of the cross‐β structure in prion fibrils: A search by seeding and electron spin resonance spectroscopy.
Chu BKY, Tsai RF, Hung CL, Kuo YH, Chen EH., Chiang YW*, Chan SI*, Chen RP*
Protein Science (2022)
A Systematic Study of the Stability, Safety, and Efficacy of the de novo Designed Antimicrobial Peptide PepD2 and Its Modified Derivatives Against Acinetobacter baumannii.
Chen SP, Chen EH, Yang SY, Kuo PS, Jan HM, Yang TC, Hsieh MY, Lee KT, Lin CH , Chen RP*
Frontiers in Microbiology (2021)
An intranasally delivered peptide drug ameliorates cognitive decline in Alzheimer transgenic mice.
Cheng YS, Chen ZT, Liao TY, Lin C, Shen HC, Wang YH, Chang CW, Liu RS, Chen RP, Tu PH
EMBO molecular medicine (2017)
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)
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)
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)