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

Omar M.A. El-Agnaf; Hazel Goodwin; Joseph M. Sheridan; Emma R. Frears; Brian M. Austen

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

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

^*Corresponding author for this work

St. George's University of London

Research output: Contribution to journal › Article › peer-review

18 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 language	English
Pages (from-to)	1-8
Number of pages	8
Journal	Protein and Peptide Letters
Volume	7
Issue number	1
Publication status	Published - 2000
Externally published	Yes

Cite this

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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.",

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AU - El-Agnaf, Omar M.A.

AU - Goodwin, Hazel

AU - Sheridan, Joseph M.

AU - Frears, Emma R.

AU - Austen, Brian M.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0002931434&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0002931434

SN - 0929-8665

VL - 7

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EP - 8

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

IS - 1

ER -

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

Abstract

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