Ramesh, J and Madhav, TR and Vatsala, S and Ramakrishna, T and Easwaran, KRK and Guillard, O and Deloncle, R (1999) Interaction of A beta peptide (1-40) with amino acid aluminium complexes: relevance to Alzheimer's disease. In: Alzheimers Reports, 2 (1). pp. 31-35.Full text not available from this repository.
A beta (39-43 aminoacid residues) is the principal peptide component of amyloid deposits in Alzheimer's disease (AD). A beta peptide is derived from the amyloid precursor protein (APP) in which mutations give rise to many forms of familial AD. Aluminium is reported to play a key role in inducing conformational change in the synthetic beta-amyloid peptide (1-40)from alpha-helix to beta-pleated sheet, leading to aggregation and fibrillar formation. We have studied the interaction of amino acid-Al complexes such as D-Asp-Al and L-Glu-Al with A beta(1-40) in TFE/buffer (70% TFE and 30% H2O v/v pH 6.7) mixture using CD spectroscopy. The interaction of either of these amino acid complexes with A beta(1-40) results in loss of alpha-helical content and the peptide is more unstructured compared to free Al3+ in the solution. Our data strongly support the idea, that the Al3+ in the form of aminoacid-Al complexes is more effective in inducing random coil conformation in the A beta peptide than the free Al3+ present in the solution.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Alzheimers Reports.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||23 Jun 2011 07:00|
|Last Modified:||23 Jun 2011 07:00|
Actions (login required)