Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences
| Title | Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences |
| Publication Type | Journal Article |
| Year of Publication | 2005 |
| Authors | Tartaglia G.G, Cavalli A., Pellarin R., Caflisch A. |
| Journal | Protein Science |
| Volume | 14 |
| Issue | 10 |
| Pagination | 2723-2734 |
| Date Published | 2005 Oct |
| Type of Article | Research Article |
| Keywords | Alzheimer Disease, Amino Acid Sequence, Amyloid, Drug Design, Humans, Models, Chemical, Parkinson Disease, Prions, Protein Denaturation, Protein Structure, Secondary |
| Abstract | The reliable identification of β-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 β-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 β-sheet organization in fibrils. The model recognizes different β-aggregating segments in mammalian and nonmammalian prion proteins, providing insights into the species barrier for the transmission of the prion disease. |
| DOI | 10.1110/ps.051471205 |
| pubindex | 0069 |
| Alternate Journal | Protein Sci. |
| PubMed ID | 16195556 |
| PubMed Central ID | PMC2253302 |
