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Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide

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Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide. / Clements, A; Walsh, D M; Williams, C H et al.
In: Neuroscience Letters, Vol. 161, No. 1, 14.10.1993, p. 17-20.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Clements, A, Walsh, DM, Williams, CH & Allsop, D 1993, 'Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide', Neuroscience Letters, vol. 161, no. 1, pp. 17-20. https://doi.org/10.1016/0304-3940(93)90129-9

APA

Clements, A., Walsh, D. M., Williams, C. H., & Allsop, D. (1993). Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide. Neuroscience Letters, 161(1), 17-20. https://doi.org/10.1016/0304-3940(93)90129-9

Vancouver

Clements A, Walsh DM, Williams CH, Allsop D. Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide. Neuroscience Letters. 1993 Oct 14;161(1):17-20. doi: 10.1016/0304-3940(93)90129-9

Author

Clements, A ; Walsh, D M ; Williams, C H et al. / Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide. In: Neuroscience Letters. 1993 ; Vol. 161, No. 1. pp. 17-20.

Bibtex

@article{f3a3f4a311b2405e81da0eeff21861ff,
title = "Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide",
abstract = "We assessed the fibrillogenic properties of synthetic peptides corresponding to residues 13-26 of beta/A4 amyloid, containing either the normal sequence (beta 13 26) or the mutations Glu22 to Gln (beta 13-26Q22) and Ala21 to Gly (beta 13-26G21). The kinetics of aggregation were monitored at 37 degrees C and pH 7.4 by measuring the amount of peptide remaining in solution, using reverse-phase high performance liquid chromatography. Negative stain electron microscopy revealed that all of the peptides formed fibrils. However, beta 13-26Q22 showed greatly accelerated fibril formation compared to the other two. The results suggest that the Q22 mutation confers increased amyloidogenic properties on the beta/A4 peptide, whereas the G21 mutation acts by a different pathogenic mechanism.",
keywords = "Alanine, Alzheimer Disease, Amino Acid Sequence, Amyloid, Amyloid beta-Peptides, Glutamates, Glutamic Acid, Glycine, Humans, Molecular Sequence Data, Mutation",
author = "A Clements and Walsh, {D M} and Williams, {C H} and D Allsop",
year = "1993",
month = oct,
day = "14",
doi = "10.1016/0304-3940(93)90129-9",
language = "English",
volume = "161",
pages = "17--20",
journal = "Neuroscience Letters",
issn = "0304-3940",
publisher = "ELSEVIER IRELAND LTD",
number = "1",

}

RIS

TY - JOUR

T1 - Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide

AU - Clements, A

AU - Walsh, D M

AU - Williams, C H

AU - Allsop, D

PY - 1993/10/14

Y1 - 1993/10/14

N2 - We assessed the fibrillogenic properties of synthetic peptides corresponding to residues 13-26 of beta/A4 amyloid, containing either the normal sequence (beta 13 26) or the mutations Glu22 to Gln (beta 13-26Q22) and Ala21 to Gly (beta 13-26G21). The kinetics of aggregation were monitored at 37 degrees C and pH 7.4 by measuring the amount of peptide remaining in solution, using reverse-phase high performance liquid chromatography. Negative stain electron microscopy revealed that all of the peptides formed fibrils. However, beta 13-26Q22 showed greatly accelerated fibril formation compared to the other two. The results suggest that the Q22 mutation confers increased amyloidogenic properties on the beta/A4 peptide, whereas the G21 mutation acts by a different pathogenic mechanism.

AB - We assessed the fibrillogenic properties of synthetic peptides corresponding to residues 13-26 of beta/A4 amyloid, containing either the normal sequence (beta 13 26) or the mutations Glu22 to Gln (beta 13-26Q22) and Ala21 to Gly (beta 13-26G21). The kinetics of aggregation were monitored at 37 degrees C and pH 7.4 by measuring the amount of peptide remaining in solution, using reverse-phase high performance liquid chromatography. Negative stain electron microscopy revealed that all of the peptides formed fibrils. However, beta 13-26Q22 showed greatly accelerated fibril formation compared to the other two. The results suggest that the Q22 mutation confers increased amyloidogenic properties on the beta/A4 peptide, whereas the G21 mutation acts by a different pathogenic mechanism.

KW - Alanine

KW - Alzheimer Disease

KW - Amino Acid Sequence

KW - Amyloid

KW - Amyloid beta-Peptides

KW - Glutamates

KW - Glutamic Acid

KW - Glycine

KW - Humans

KW - Molecular Sequence Data

KW - Mutation

U2 - 10.1016/0304-3940(93)90129-9

DO - 10.1016/0304-3940(93)90129-9

M3 - Journal article

C2 - 7902973

VL - 161

SP - 17

EP - 20

JO - Neuroscience Letters

JF - Neuroscience Letters

SN - 0304-3940

IS - 1

ER -