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Previous studies revealed that copper complexes of amyloid beta (A\u03b2) peptides, mainly the A\u03b2\n                    <jats:sub>1\u2010x<\/jats:sub>\n                    form, could effectively catalyze the production of reactive oxygen species (ROS), causing the oxidation of physiological compounds. The Cu(II) binding to N\u2010truncated A\u03b2 forms containing His\u20102 and His\u20103 motifs produced less oxidative damage by arresting the Cu(II) ions in highly stable Cu(II)\/A\u03b2 complexes. This could be reversed, however, by interactions with low molecular weight (LMW) substances. In this work, we investigated the influence of biologically relevant LMW: His\u20101 dipeptide His\u2010Leu, histidine, imidazole, and neurotransmitters histamine, glycine, and glutamate on the ROS\u2010related ascorbate oxidation by Cu(II) complexes of A\u03b2 peptides comprising the His\u20102 and His\u20103 motifs, namely A\u03b2\n                    <jats:sub>4\u20109<\/jats:sub>\n                    , A\u03b2\n                    <jats:sub>5\u20109<\/jats:sub>\n                    , and A\u03b2\n                    <jats:sub>12\u201016<\/jats:sub>\n                    . These peptides are putative products of A\u03b2 hydrolysis by protease neprilysin. A significantly higher efficiency in the ascorbate oxidation was observed for the ternary Cu(II)\/A\u03b2\/LMW systems with His\u2010Leu and histidine compared to the binary Cu(II)\/A\u03b2 complexes. The effect was more pronounced for the systems with A\u03b2\n                    <jats:sub>4\u20109<\/jats:sub>\n                    (the His\u20103 motif only) than those with A\u03b2\n                    <jats:sub>5\u20109<\/jats:sub>\n                    and A\u03b2\n                    <jats:sub>12\u201016<\/jats:sub>\n                    (containing the His\u20102 motif), which is likely connected with a faster Cu(II) trapping by the His\u20102 peptides compared to the His\u20103 peptides. The obtained results raise further questions regarding the copper redox activity in Alzheimer's disease.\n                    <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                      <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc70145-fig-0010-m.png\">\n                        <jats:alt-text>image<\/jats:alt-text>\n                      <\/jats:graphic>\n                    <\/jats:boxed-text>\n                  <\/jats:p>","DOI":"10.1111\/jnc.70145","type":"journal-article","created":{"date-parts":[[2025,7,14]],"date-time":"2025-07-14T06:31:51Z","timestamp":1752474711000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Oxidative Activity of Copper Ions in Ternary Systems With N\u2010Truncated Amyloid Beta Peptides and Low Molecular Weight Substances"],"prefix":"10.1111","volume":"169","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8890-9435","authenticated-orcid":false,"given":"Dobromi\u0142a","family":"Sudzik","sequence":"first","affiliation":[{"name":"Chair of Medical Biotechnology, Faculty of Chemistry Warsaw University of Technology  Warsaw Poland"},{"name":"Institute of Biochemistry and Biophysics Polish Academy of Sciences  Warsaw Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3780-083X","authenticated-orcid":false,"given":"Wojciech","family":"Bal","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Biophysics Polish Academy of Sciences  Warsaw Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6206-4195","authenticated-orcid":false,"given":"Nina E.","family":"Wezynfeld","sequence":"additional","affiliation":[{"name":"Chair of Medical Biotechnology, Faculty of Chemistry Warsaw University of Technology  Warsaw Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2025,7,13]]},"reference":[{"key":"e_1_2_10_2_1","volume-title":"2024 Alzheimer's Disease Facts and Figures","author":"Alzheimer's Association","year":"2024"},{"key":"e_1_2_10_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.analchem.8b00740"},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF02430602"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jinorgbio.2024.112775"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.inorgchem.9b03153"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.inorgchem.6b01441"},{"key":"e_1_2_10_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.inorgchem.8b03051"},{"key":"e_1_2_10_9_1","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21176190"},{"key":"e_1_2_10_10_1","doi-asserted-by":"publisher","DOI":"10.1039\/C9MT00236G"},{"key":"e_1_2_10_11_1","volume-title":"Fmoc Solid Phase Peptide Synthesis","author":"Chan W. 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