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We synthesized conjugates of amiridine and salicylimine\/amine\n                    <jats:bold>9, 10<\/jats:bold>\n                    with linkers containing an\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acyl group at the amiridine fragment as analogs of our previously obtained hybrids\n                    <jats:bold>1, 2<\/jats:bold>\n                    containing an\n                    <jats:italic>N<\/jats:italic>\n                    \u2010aminohexamethylene spacer. A comparative study of selected biological activities of\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acylalkylene conjugates\n                    <jats:bold>9, 10<\/jats:bold>\n                    with conjugates\n                    <jats:bold>1, 2<\/jats:bold>\n                    showed substantial decreases in anti\u2010butyrylcholinesterase (BChE) activity (35\u2010fold for the imine and 8\u2010fold for the amine), loss of anti\u2010acetylcholinesterase (AChE) activity, and disappearance of the ability to block amyloid beta (1\u201342) (A\u03b2\n                    <jats:sub>42<\/jats:sub>\n                    ) self\u2010aggregation. Similar effects were observed for the model compound\n                    <jats:italic>N<\/jats:italic>\n                    \u2010hexylamiridine\n                    <jats:bold>3<\/jats:bold>\n                    and its\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acyl derivative\n                    <jats:bold>11<\/jats:bold>\n                    . However,\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acyl functionalization at the amiridine pharmacophore did not reduce the ability of the conjugates to block AChE\u2010induced \u03b2\u2010amyloid aggregation and only slightly decreased their antiradical activity, maintaining the higher activity of amines compared to imines. These effects were consistent with results from quantum mechanical calculations and molecular docking, showing that\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acylation of amiridine decreased the proton affinity of its endocyclic N\u2010atom. Consequently, the amiridine pharmacophore was essentially unprotonated, thereby diminishing the anticholinesterase activity of conjugates\n                    <jats:bold>9<\/jats:bold>\n                    and\n                    <jats:bold>10<\/jats:bold>\n                    and their ability to block A\u03b2\n                    <jats:sub>42<\/jats:sub>\n                    self\u2010aggregation.\n                  <\/jats:p>","DOI":"10.1002\/cmdc.70392","type":"journal-article","created":{"date-parts":[[2026,7,25]],"date-time":"2026-07-25T02:37:18Z","timestamp":1784947038000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Influence of\n                    <i>N<\/i>\n                    \u2010Functionalization of Amiridine on the Biological Activity of Its Conjugates as Multitarget Agents for Potential Treatment of Alzheimer's 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