Kametani, F and Tanaka, K and Tokuda, T and Allsop, D (1995) The immunoreactive profile at the N-terminal region of Aβ1-39/40 but not Aβ1-42 changes with transition from monomer/dimer to further peptide aggregates. Brain Research, 703 (1-2). pp. 237-241. ISSN 0006-8993Full text not available from this repository.
Using site-specific antibodies, we assessed the effect of aggregation of various length forms of A beta on the immunoreactive profile of the peptides. All of the antibodies tested reacted with monomeric/dimeric forms of A beta 1-42 and its further aggregates. However, antibodies directed against the 1-24 region of A beta reacted weakly or not at all with A beta 1-39/40 monomers or dimers, but immunoreactivity was enhanced substantially following peptide incubation and aggregation. These results suggest that the conformation of the N-terminal region of monomeric and dimeric A beta 1-39/40 is different from that of aggregated forms, whereas the longer A beta 1-42 does not significantly change its N-terminal conformation during beta-sheet fibril formation. These immunochemical results are consistent with previous structural data, and help to explain the differential effects of A beta 1-39/40 and 1-42 on fibril formation in brain.
|Journal or Publication Title:||Brain Research|
|Uncontrolled Keywords:||Blotting, Western ; Immunoenzyme Techniques ; Peptide Fragments ; Protein Conformation|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited On:||07 Nov 2011 13:56|
|Last Modified:||03 Nov 2015 15:08|
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