Copper-assisted interaction between amyloid-β and prion: Ternary metal complexes with Aβ N-terminus and octarepeat
| Autor: | Giuseppe Di Natale, Antonio Magrì, Enrico Rizzarelli |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Stereochemistry chemistry.chemical_element Zinc Inorganic Chemistry Metal 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Deprotonation Amide Materials Chemistry Physical and Theoretical Chemistry Histidine A? ESI-MS Copper N-terminus Crystallography 030104 developmental biology chemistry visual_art Potentiometry Prion visual_art.visual_art_medium Copper(II) complexes Ternary operation 030217 neurology & neurosurgery |
| Zdroj: | Inorganica Chimica Acta (Testo stamp.) 472 (2018): 93–102. doi:10.1016/j.ica.2017.10.032 info:cnr-pdr/source/autori:Magri A.; Di Natale G.; Rizzarelli E./titolo:Copper-assisted interaction between amyloid-? and prion: Ternary metal complexes with A? N-terminus and octarepeat/doi:10.1016%2Fj.ica.2017.10.032/rivista:Inorganica Chimica Acta (Testo stamp.)/anno:2018/pagina_da:93/pagina_a:102/intervallo_pagine:93–102/volume:472 |
| ISSN: | 0020-1693 |
| DOI: | 10.1016/j.ica.2017.10.032 |
| Popis: | Alzheimer and prion diseases are neurodegenerative disorders in which amyloid-beta (Aβ) and prion protein (PrP), respectively, failed their normal functions inducing cellular apoptosis. Histidine-based high-affinity metal-binding sites in the N-terminus domains, which favor the binding of transition metals such as copper and zinc, feature both Aβ and PrP. Recently, the biological role of copper(II) on the two protein interaction has been revealed. Many studies have been focused on copper(II) binding affinity for both Aβ or prion protein while ternary complexes formed by this metal with both proteins have not been investigated. Here we report a combined ESI MS, potentiometric and spectroscopic (CD, UV-Vis) study on ternary complexes formed by copper(II) ion with Aβ and PrP peptides fragments containing potential metal binding sites. In particular, Aβ(1-4), Aβ(1-6), Ac-Aβ(1-6), Aβ(1-16)PEG and the octarepeat (PHGGGWGQ) of prion protein were studied. ESI-MS results indicate that the formation of 1:1:1 ternary complexes occurred at the physiological pH range. Potentiometric and spectroscopic data demonstrate that in a large pH range, ternary species prevail over binary species with the histidine-driven amide deprotonation. |
| Databáze: | OpenAIRE |
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