Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases

Omar Ali El-Agnaf, Hazel Goodwin, Joseph M. Sheridan, Emma R. Frears, Brian M. Austen

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

β-Amyloid protein, the α-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.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalProtein and Peptide Letters
Volume7
Issue number1
Publication statusPublished - 2000
Externally publishedYes

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Neurodegenerative diseases
Amyloidogenic Proteins
Solid-Phase Synthesis Techniques
Neurodegenerative Diseases
Synucleins
Peptides
Amyloid
Peptide Hydrolases
Agglomeration
Resins
Proteins
Prion Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases. / Ali El-Agnaf, Omar; Goodwin, Hazel; Sheridan, Joseph M.; Frears, Emma R.; Austen, Brian M.

In: Protein and Peptide Letters, Vol. 7, No. 1, 2000, p. 1-8.

Research output: Contribution to journalArticle

Ali El-Agnaf, Omar ; Goodwin, Hazel ; Sheridan, Joseph M. ; Frears, Emma R. ; Austen, Brian M. / Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases. In: Protein and Peptide Letters. 2000 ; Vol. 7, No. 1. pp. 1-8.
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