The N-terminal fragment of Aβ (β = beta) peptide is able to bind essential transition metal ions like, copper, zinc and iron. Metal binding usually occurs via the imidazole nitrogens of the three His residues which play a key role in the coordination chemistry. Among all the investigated systems, the interaction between copper and Amyloid β assume a biological relevance because of the interplay between the two copper oxidation states, Cu(II) and Cu(I), and their involvement in redox reactions. Both copper ions share the ability to bind Amyloid β. A huge number of investigations have demonstrated that Cu(II) anchors to the N-terminal amino and His6, His13/14 imidazole groups, while Cu(I) forms a linear complex by coordinating to the His13 and His14 dyad. In this study we have analyzed Cu(I) interaction with the Amyloid β fragment encompassing the first 16 amino-acids. Our data were obtained by means of NMR spectroscopy which provided relevant structural details of the metal complexes. Our findings are consistent with the involvement of two or three His in the Cu(I) coordination sphere and indicate that His6 effectively participates to the metal binding.
|Titolo:||Structural analysis of copper(I) interaction with amyloid β peptide|
VALENSIN, DANIELA (Corresponding)
|Citazione:||De Gregorio, G., Biasotto, F., Hecel, A., Luczkowski, M., Kozlowski, H., & Valensin, D. (2019). Structural analysis of copper(I) interaction with amyloid β peptide. JOURNAL OF INORGANIC BIOCHEMISTRY, 195, 31-38.|
|Appare nelle tipologie:||1.1 Articolo in rivista|
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