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 0304-3940Full text not available from this repository.
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.
|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|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited On:||07 Nov 2011 16:57|
|Last Modified:||13 Jan 2016 13:51|
Actions (login required)