HOME- R&D
- Bryn Mawr Conference
- Hyderabad Conference
- Workshops & Training
- Program
- Drug Discovery Innovation
- Proteins
- Abstracts
- Speakers
- Buldyrev, S
- Daura, X
- Ding, F
- Dixon, R
- Dokholyan, N
- Duan, Y
- Fasnacht, M
- Kiefhaber, T
- Miranker, A
- Pande, V
- Pitera, J
- Shea, J
- Teplow, D
- Tiana, G
- van Gunsteren, W
- Vendruscola, M
- Wenzel, W
- Winn, P
- Zhou, R
- Quantum Biochemistry
- Screening
- Web Services
- Pharmacophores
- Graph Mining
- Nanotech
- Membranes & Ion Channels
- Exhibition
- Registration
- Jobs
- Contact
- Schedule
|
|
|
|
|
|
|
| Joan-Emma Shea, University of California, Santa Barbara |
|
| Joan-Emma Shea received her B.Sc. in chemistry from McGill University (Canada) in 1992 and her Ph.D. in physical chemistry from the Massachusetts Institute of Technology in 1997. She pursued her postdoctoral studies jointly in the department of molecular biology at the Scripps Research Institute and in the department of physics at the University of California, San Diego. After a year as an assistant professor of chemistry at the University of Chicago, she joined the department of chemistry and biochemistry at the University of California, Santa Barbara in 2001. Her research focuses on developing and applying the techniques of statistical and computational physics to the study of biological problems. Current work involves the investigation of cellular processes such as in-vivo protein folding and protein aggregation. She is the recipient of an NSF Career Award, the David and Lucile Packard Award and an Alfred P. Sloan research fellowship.
|
|
Simulations of peptide inhibitors of Amyloid-beta fibrillogenesis
Joan-Emma Shea, University of California, Santa Barbara
Alzheimer's disease is associated with the abnormal self-assembly of the Alzheimer Amyloid-beta (A beta) peptide into aggregate structures. Both the end-product amyloid fibrils as well as smaller soluble oligomers formed in the initial stages of aggregation appear to be toxic to the cell. An attractive therapeutic approach to combat amyloid diseases lies in the development of strategies to inhibit or reverse aggregation. We consider in this work the 16-22 fragment of the (A beta) peptide, the shortest sequence of Alzheimer A beta peptides capable of forming toxic fibrils. An N-methylated version of this peptide has recently been shown to inhibit fibrillogenesis and disassemble A beta fibrils. We present molecular dynamics simulations of the interaction of this inhibitor peptide with a model A beta fibril and propose a novel mechanism for its mode of action. Implications for the design of further amyloid inhibitors will be discussed.
|
|
|
|
|
|
|
|
|
