©ARC Page | 28 Conformational Studies of Aβ (1-12) with Metals and Small Molecules Suggests Plausible Disruption of Aggregation

Abstract: Alzheimer’s disease (AD), the most common form of senile dementia, is associated with the progressive accumulation of plaques and tangles within the neuronal cell. The plaques are composed of amyloid (Aβ) peptide fragments with a high propensity for aggregation. Metal ion binding to Aβ peptide has been known to alter the aggregation of the peptide and to be involved in the pathogenecity of Alzheimer’s. Earlier investigations suggest that the N terminal hydrophilic region of the peptide exhibit preferential ligand binding capabilities and, thus initiate the onset of aggregation events. The complexation events with metals like zinc, copper, aluminium, and small molecules like betaine and curcumin, reported in this paper provide a molecular level appreciation of the binding characteristics of the Aβ (1-12) peptide fragments and the variations thereof. Our data show notable conformational changes induced due the binding of these ligands, suggesting plausible clues to explore these molecules as potential inhibitors an