Department of Chemistry and Biochemistry
Ph.D., University of Pennsylvania
Office: PS 301G
Phone: (561) 297-0094
The research in our lab is on biochemistry and molecular biophysics, problems of protein folding, misfolding and aggregation, biomaterials, and biosensor. The research is directed towards understanding the structure, function and conformational dynamics of proteins. One of the aims is to understand the basic principles that govern protein folding in cellular environment and to explore the underlying mechanisms of amyloid diseases caused by protein misfolding and aggregation.
1. Elbassal, E. A., Liu, H., Morris, C., Wojcikiewicz, E. P., & Du, D.* “Effects of charged cholesterol derivatives on Aβ40 amyloid formation.” J. Phys. Chem. B., 2016, 120, 59-68.
2. Liu, H., Ojha, B., Morris, C., Jiang, M., Wojcikiewicz, E. P., Rao, P. P. & Du, D.* “Positively charged chitosan and N-trimethyl chitosan inhibit Aβ40 fibrillogenesis.” Biomacromolecules, 2015, 16, 2363-2373.
3. Liu, H., Lantz, R., Cosme, P., Rivera, N., Andino, C., Gonzalez, W. G., Terentis, A. C., Wojcikiewicz, E. P., Oyola, R., Miksovska, J. & Du, D.* “Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ1-23 using an unnatural amino acid.” Chem. Commun. 2015, 51, 7000-7003.
4. Markiewicz, B. N., Oyola, R., Du, D.* & Gai, F.* “Aggregation gatekeeper and controlled assembly of Trpzip β-hairpins.” Biochemistry 2014, 53, 1146-1154.
5. Ojha, B., Liu, H., Dutta, S., Rao, P. P., Wojcikiewicz, W. P. & Du, D.* “Poly(4-styrenesulfonate) as an inhibitor of Abeta40 amyloid fibril formation.” J. Phys. Chem. B. 2013, 117, 13975-13984.