Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid.

The anomalous interaction between metal ions and the peptide beta-amyloid is one of the hallmarks of Alzheimer's disease. Metal-binding biopolymers, including polysaccharides, can elucidate the fundamental aspects of metal ions' interactions with biological tissue and their interplay in Alzheimer's disease. This work focuses on the role of the alginate composition on Cu(II) adsorption in the presence of histidine or β-amyloid, the peptide associated with the progression of Alzheimer's disease.

Amino acid-functionalized chitosan beads for in vitro copper ions uptake in the presence of histidine.

One of the hallmarks of Alzheimer's Disease (AD) is the anomalous binding involving amyloid-β (Aβ) peptide and metal ions, such as copper, formed through histidine (His) residues. Herein, adsorption experiments were performed to test the in vitro ability of chitosan to uptake copper ions in the presence of histidine. The characterization of the beads was assessed before and after the adsorption process by scanning electron microscope, X-ray diffraction and Fourier-transform infrared spectroscopy.

Copper Ion Uptake by Chitosan in the Presence of Amyloid-β and Histidine.

Alzheimer's disease (AD) is related to the anomalous binding that occurs between amyloid-β peptide (Aβ) and copper ion, through imidazole ring of histidine (His), as stated in the literature. It is also known that high-affinity metal ion chelators can be pharmacologically used as a possible therapeutic approach. In this work, we tested the ability "in vitro" of chitosan (Chi) to reduce Aβ aggregation and Thioflavin T binding assay indicated that chitosan has affinity for Aβ and interferes in its aggregation.