Synthesis of peptide sequences derived from fibril-forming proteins
Date
2011
Authors
Scanlon, D.
Karas, J.
Editors
Hill, A.F.
Barnham, K.J.
Bottomley, S.P.
Cappai, R.
Barnham, K.J.
Bottomley, S.P.
Cappai, R.
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
Methods in Molecular Biology, 2011; 752:29-43
Statement of Responsibility
Denis B. Scanlon and John A. Karas
Conference Name
Abstract
The pathogenesis of a large number of diseases, including Alzheimer's Disease, Parkinson's Disease, and Creutzfeldt-Jakob Disease (CJD), is associated with protein aggregation and the formation of amyloid, fibrillar deposits. Peptide fragments of amyloid-forming proteins have been found to form fibrils in their own right and have become important tools for unlocking the mechanism of amyloid fibril formation and the pathogenesis of amyloid diseases. The synthesis and purification of peptide sequences derived from amyloid fibril-forming proteins can be extremely challenging. The synthesis may not proceed well, generating a very low quality crude product which can be difficult to purify. Even clean crude peptides can be difficult to purify, as they are often insoluble or form fibrils rapidly in solution. This chapter presents methods to recognise and to overcome the difficulties associated with the synthesis, and purification of fibril-forming peptides, illustrating the points with three synthetic examples.
School/Discipline
School of Chemistry and Physics
Dissertation Note
Provenance
Description
Also published as a book chapter: Protein Folding, Misfolding, and Disease: Methods and Protocols, 2011 / A. F. Hill, K. J. Barnham, S. P. Bottomley & R. Cappai (eds.), Ch.3 pp.29-43
Access Status
Rights
© Springer Science+Business Media, LLC 2011