{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T00:48:46Z","timestamp":1785372526880,"version":"3.55.0"},"reference-count":42,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2021,5,14]],"date-time":"2021-05-14T00:00:00Z","timestamp":1620950400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003407","name":"Ministero dell\u2019Istruzione, dell\u2019Universit\u00e0 e della Ricerca","doi-asserted-by":"publisher","award":["Research Projects of National Interest (PRIN) 2015 prot. 2015T778JW."],"award-info":[{"award-number":["Research Projects of National Interest (PRIN) 2015 prot. 2015T778JW."]}],"id":[{"id":"10.13039\/501100003407","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The redox chemistry of copper(II) is strongly modulated by the coordination to amyloid-\u03b2 peptides and by the stability of the resulting complexes. Amino-terminal copper and nickel binding motifs (ATCUN) identified in truncated A\u03b2 sequences starting with Phe4 show very high affinity for copper(II) ions. Herein, we study the oxidase activity of [Cu\u2013A\u03b24\u2212x] and [Cu\u2013A\u03b21\u2212x] complexes toward dopamine and other catechols. The results show that the CuII\u2013ATCUN site is not redox-inert; the reduction of the metal is induced by coordination of catechol to the metal and occurs through an inner sphere reaction. The generation of a ternary [CuII\u2013A\u03b2\u2013catechol] species determines the efficiency of the oxidation, although the reaction rate is ruled by reoxidation of the CuI complex. In addition to the N-terminal coordination site, the two vicinal histidines, His13 and His14, provide a second Cu-binding motif. Catechol oxidation studies together with structural insight from the mixed dinuclear complexes Ni\/Cu\u2013A\u03b24\u2212x reveal that the His-tandem is able to bind CuII ions independently of the ATCUN site, but the N-terminal metal complexation reduces the conformational mobility of the peptide chain, preventing the binding and oxidative reactivity toward catechol of CuII bound to the secondary site.<\/jats:p>","DOI":"10.3390\/ijms22105190","type":"journal-article","created":{"date-parts":[[2021,5,14]],"date-time":"2021-05-14T10:54:22Z","timestamp":1620989662000},"page":"5190","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Oxidase Reactivity of CuII Bound to N-Truncated A\u03b2 Peptides Promoted by Dopamine"],"prefix":"10.3390","volume":"22","author":[{"given":"Chiara","family":"Bacchella","sequence":"first","affiliation":[{"name":"Dipartimento di Chimica, Universit\u00e0 di Pavia, Via Taramelli 12, 27100 Pavia, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1231-4045","authenticated-orcid":false,"given":"Simone","family":"Dell\u2019Acqua","sequence":"additional","affiliation":[{"name":"Dipartimento di Chimica, Universit\u00e0 di Pavia, Via Taramelli 12, 27100 Pavia, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6618-7555","authenticated-orcid":false,"given":"Stefania","family":"Nicolis","sequence":"additional","affiliation":[{"name":"Dipartimento di Chimica, Universit\u00e0 di Pavia, Via Taramelli 12, 27100 Pavia, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8791-6446","authenticated-orcid":false,"given":"Enrico","family":"Monzani","sequence":"additional","affiliation":[{"name":"Dipartimento di Chimica, Universit\u00e0 di Pavia, Via Taramelli 12, 27100 Pavia, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7671-0506","authenticated-orcid":false,"given":"Luigi","family":"Casella","sequence":"additional","affiliation":[{"name":"Dipartimento di Chimica, Universit\u00e0 di Pavia, Via Taramelli 12, 27100 Pavia, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,5,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/S0140-6736(15)01124-1","article-title":"Alzheimer\u2019s disease","volume":"388","author":"Scheltens","year":"2016","journal-title":"Lancet"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1152\/physrev.2001.81.2.741","article-title":"Alzheimer\u2019s disease: Genes, proteins, and therapy","volume":"81","author":"Selkoe","year":"2001","journal-title":"Physiol. 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