What is it about?
Folding and self-assembly of amyloid beta (Ab) peptide are linked to Alzheimer’s disease. To understand the initial stage of amyloid-b peptide aggregation, energies and conformational characteristics of monomers of Ab fragment Ab(28–35) and its mutants formed by single amino acid substitution of Ala30 by Gly30 (A30G) as well as Ile30 (A30I), are investigated using density functional theory calculations and experimental studies.
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Why is it important?
Quantum chemical calculations in aqueous medium predict that the random coil conformer possesses the lowest energy in both Ab(28–35) and A30I in agreement with earlier experimental observation in the freshly dissolved monomers (Nagarajan et al FEBS J. 275, 2415–2427)
Perspectives
The prediction of low energy differences among the conformers in the aqueous medium leads to the inference that the helical and strand conformers of Ab(28– 35) and its mutants can readily function as intermediate structures which can accelerate the rate of amyloid formation.
E.J. Padma Malar
University of Madras
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This page is a summary of: Density functional theory analysis and spectral studies on amyloid peptide Aβ(28–35) and its mutants A30G and A30I, Journal of Structural Biology, June 2010, Elsevier,
DOI: 10.1016/j.jsb.2010.02.017.
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