{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T16:52:08Z","timestamp":1791996728627,"version":"4.4.0"},"reference-count":44,"publisher":"National Academy of Sciences","issue":"23","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2006,6,6]]},"abstract":"<jats:p>\n                    In Alzheimer\u2019s disease, both acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) colocalize with brain fibrils of amyloid-\u03b2 (A\u03b2) peptides, and synaptic AChE-S facilitates fibril formation by association with insoluble A\u03b2 fibrils. Here, we report that human BChE and BSP41, a synthetic peptide derived from the BChE C terminus, inversely associate with the soluble A\u03b2 conformers and delay the onset and decrease the rate of A\u03b2 fibril formation\n                    <jats:italic>in vitro<\/jats:italic>\n                    , at a 1:100 BChE\/A\u03b2 molar ratio and in a dose-dependent manner. The corresponding AChE synthetic peptide (ASP)40 peptide, derived from the homologous C terminus of synaptic human (h)AChE-S, failed to significantly affect A\u03b2 fibril formation, attributing the role of enhancing this process to an AChE domain other than the C terminus. Circular dichroism and molecular modeling confirmed that both ASP40 and BChE synthetic peptide (BSP)41 are amphipathic \u03b1-helices. However, ASP40 shows symmetric amphipathicity, whereas BSP41 presented an aromatic tryptophan residue in the polar side of the C terminus. That this aromatic residue is causally involved in the attenuating effect of BChE was further supported by mutagenesis experiments in which (W8R) BSP41 showed suppressed capacity to attenuate fibril formation. In Alzheimer\u2019s disease, BChE may have thus acquired an inverse role to that of AChE by adopting imperfect amphipathic characteristics of its C terminus.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0602922103","type":"journal-article","created":{"date-parts":[[2006,5,26]],"date-time":"2006-05-26T20:55:59Z","timestamp":1148676959000},"page":"8628-8633","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":146,"title":["Butyrylcholinesterase attenuates amyloid fibril formation\n                    <i>in vitro<\/i>"],"prefix":"10.1073","volume":"103","author":[{"given":"Sophia","family":"Diamant","sequence":"first","affiliation":[{"name":"Departments of *Biological and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erez","family":"Podoly","sequence":"additional","affiliation":[{"name":"the Wolfson Centre for Applied Structural Biology, Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Assaf","family":"Friedler","sequence":"additional","affiliation":[{"name":"Organic Chemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hagai","family":"Ligumsky","sequence":"additional","affiliation":[{"name":"Departments of *Biological and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oded","family":"Livnah","sequence":"additional","affiliation":[{"name":"the Wolfson Centre for Applied Structural Biology, Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hermona","family":"Soreq","sequence":"additional","affiliation":[{"name":"Departments of *Biological and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2006,6,6]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.31.18295"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.36.25945"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.35.22364"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M210207200"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1678899"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1006\/nbdi.2001.0462"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/cne.10751"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1002\/ana.410360506"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M103192200"},{"key":"e_1_3_3_10_2","first-page":"359","volume":"1","author":"Inestrosa N. 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