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. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society.
Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences / Tartaglia, G. G.; Cavalli, A.; Pellarin, R.; Caflisch, A.. - In: PROTEIN SCIENCE. - ISSN 0961-8368. - 14:10(2005), pp. 2723-2734. [10.1110/ps.051471205]
Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences
Tartaglia, G. G.;
2005
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. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society.File | Dimensione | Formato | |
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