Abstract
P-Amyloid protein, the a-synuclein fragment NAC, and protease-resistant forms of prion proteins are found deposited in the pathological lesions associated with neurodegenerative disease. Chemical syntheses of these proteins are notoriously difficult due to aggregation of the peptides on the resin during synthesis. We report optimised solid-phase syntheses of several amyloid peptides in high yield and >90% initial purity.
Protein & Peptide Letters
Title:Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases
Volume: 7 Issue: 1
Author(s): Joseph M Sheridan, Omar M.A. El-Agnaf, Hazel Goodwin, Emma R. Frears and Brian M. Austen*
Affiliation:
- Neurodegeneration Unit, Department of Surgery, St. George's Hospital Medical School, Cranmer Terrace, Tooting, London, SWI 7 ORE, UK
Abstract: P-Amyloid protein, the a-synuclein fragment NAC, and protease-resistant forms of prion proteins are found deposited in the pathological lesions associated with neurodegenerative disease. Chemical syntheses of these proteins are notoriously difficult due to aggregation of the peptides on the resin during synthesis. We report optimised solid-phase syntheses of several amyloid peptides in high yield and >90% initial purity.
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Cite this article as:
Sheridan M Joseph, El-Agnaf M.A. Omar, Goodwin Hazel, Frears R. Emma and Austen M. Brian*, Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases, Protein & Peptide Letters 2000; 7 (1) . https://dx.doi.org/10.2174/092986650701221205144944
DOI https://dx.doi.org/10.2174/092986650701221205144944 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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