Clements, A and Walsh, D M and Williams, C H and 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). pp. 17-20. ISSN 0304-3940
Full text not available from this repository.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.
| Item Type: | Article |
|---|---|
| Journal or Publication Title: | Neuroscience Letters |
| Uncontrolled Keywords: | Alanine ; Alzheimer Disease ; Amino Acid Sequence ; Amyloid ; Amyloid beta-Peptides ; Glutamates ; Glutamic Acid ; Glycine ; Humans ; Molecular Sequence Data ; Mutation |
| Subjects: | UNSPECIFIED |
| Departments: | Faculty of Health and Medicine > Biomedical & Life Sciences |
| ID Code: | 50844 |
| Deposited By: | ep_importer_pure |
| Deposited On: | 07 Nov 2011 16:57 |
| Refereed?: | Yes |
| Published?: | Published |
| Last Modified: | 26 Jul 2012 19:43 |
| Identification Number: | |
| URI: | http://eprints.lancs.ac.uk/id/eprint/50844 |
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