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 |
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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 |
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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 journal › Article
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TY - JOUR
T1 - Improved solid-phase syntheses of amyloid proteins associated with neurodegenerative diseases
AU - Ali El-Agnaf, Omar
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
UR - http://www.scopus.com/inward/citedby.url?scp=0002931434&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0002931434
VL - 7
SP - 1
EP - 8
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
SN - 0929-8665
IS - 1
ER -