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© Research
Publication : Protein science : a publication of the Protein Society

Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Protein science : a publication of the Protein Society - 01 Oct 2005

Tartaglia GG, Cavalli A, Pellarin R, Caflisch A

Link to Pubmed [PMID] – 16195556

Protein Sci. 2005 Oct;14(10):2723-34

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 prion proteins, providing insights into the species barrier for the transmission of the prion disease.

http://www.ncbi.nlm.nih.gov/pubmed/16195556