Journal
PROTEIN SCIENCE
Volume 14, Issue 10, Pages 2723-2734Publisher
WILEY
DOI: 10.1110/ps.051471205
Keywords
Alzheimer's disease; amyloid; protein aggregation rate; priori protein; species barrier; genetic algorithm; molecular dynamics
Categories
Ask authors/readers for more resources
The reliable identification of beta-aggregating stretches in protein sequences is essential for the development of therapeutic agents for Alzheimer's and Parkinson's diseases, as well as other pathological conditions associated with protein deposition. Here, a model based on physicochemical properties and computational design of beta-aggregating peptide sequences is shown to be able to predict the aggregation rate over a large set of natural polypeptide sequences. Furthermore, the model identifies aggregation-prone fragments within proteins and predicts the parallel or anti-parallel beta-sheet organization in fibrils. The model recognizes different beta-aggregating segments in mammalian and nonmammalian priori proteins, providing insights into the species barrier for the transmission of the priori disease.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available