{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T16:41:59Z","timestamp":1787676119400,"version":"build-2784847793"},"reference-count":99,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2022,7]]},"DOI":"10.1016\/j.ejmech.2022.114400","type":"journal-article","created":{"date-parts":[[2022,4,23]],"date-time":"2022-04-23T02:01:11Z","timestamp":1650679271000},"page":"114400","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"special_numbering":"C","title":["New A\u03b2(1\u201342) ligands from anti-amyloid antibodies: Design, synthesis, and structural interaction"],"prefix":"10.1016","volume":"237","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9690-907X","authenticated-orcid":false,"given":"Angelo","family":"Santoro","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuela","family":"Grimaldi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michela","family":"Buonocore","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ilaria","family":"Stillitano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonio","family":"Gloria","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5260-7088","authenticated-orcid":false,"given":"Matteo","family":"Santin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabrizio","family":"Bobba","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matilde","family":"Sublimi Saponetti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena","family":"Ciaglia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna Maria","family":"D'Ursi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2022.114400_bib1","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1021\/acscombsci.6b00116","article-title":"Rationally designed peptides and peptidomimetics as inhibitors of amyloid-\u03b2 (A\u03b2) aggregation: potential therapeutics of Alzheimer's disease","volume":"19","author":"Goyal","year":"2017","journal-title":"ACS Comb. Sci."},{"key":"10.1016\/j.ejmech.2022.114400_bib2","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1007\/978-94-007-5416-4_14","article-title":"Alzheimer's disease","volume":"65","author":"De-Paula","year":"2012","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.ejmech.2022.114400_bib3","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.jalz.2012.11.007","article-title":"The global prevalence of dementia: a systematic review and metaanalysis","volume":"9","author":"Prince","year":"2013","journal-title":"Alzheimer's Dementia"},{"key":"10.1016\/j.ejmech.2022.114400_bib4","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1212\/WNL.0000000000003653","article-title":"Serum neurofilament is associated with progression of brain atrophy and disability in early MS","volume":"88","author":"Kuhle","year":"2017","journal-title":"Neurology"},{"key":"10.1016\/j.ejmech.2022.114400_bib5","series-title":"The Right Therapy for Neurological Disorders","first-page":"117","article-title":"Cerebrospinal fluid biomarkers for target engagement and efficacy in clinical trials for Alzheimer's and Parkinson's diseases","author":"Parnetti","year":"2016"},{"key":"10.1016\/j.ejmech.2022.114400_bib6","series-title":"Biomarkers for Alzheimer's Disease Drug Development","first-page":"139","article-title":"Blood-based biomarker screening with agnostic biological definitions for an accurate diagnosis within the dimensional spectrum of neurodegenerative diseases","author":"Baldacci","year":"2018"},{"key":"10.1016\/j.ejmech.2022.114400_bib7","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1038\/s41582-018-0079-7","article-title":"Blood-based biomarkers for Alzheimer disease: mapping the road to the clinic","volume":"14","author":"Hampel","year":"2018","journal-title":"Nat. Rev. Neurol."},{"key":"10.1016\/j.ejmech.2022.114400_bib8","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1001\/jamaneurol.2016.0301","article-title":"Genomics of Alzheimer disease: a review","volume":"73","author":"Rosenberg","year":"2016","journal-title":"JAMA Neurol."},{"key":"10.1016\/j.ejmech.2022.114400_bib9","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","article-title":"The amyloid state of proteins in human diseases","volume":"148","author":"Eisenberg","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.ejmech.2022.114400_bib10","doi-asserted-by":"crossref","first-page":"5147","DOI":"10.1021\/cr3000994","article-title":"The amyloid beta peptide: a chemist's perspective. Role in Alzheimer's and fibrillization","volume":"112","author":"Hamley","year":"2012","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ejmech.2022.114400_bib11","doi-asserted-by":"crossref","first-page":"395","DOI":"10.3389\/fcell.2021.642623","article-title":"Membrane interactions and toxicity by misfolded protein oligomers","volume":"9","author":"Gonzalez-Garcia","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.ejmech.2022.114400_bib12","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/nature20416","article-title":"The activities of amyloids from a structural perspective","volume":"539","author":"Riek","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2022.114400_bib13","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.2174\/0929867043455549","article-title":"Pharmaceutical strategies against amyloidosis: old and new drugs in targeting a \u201cprotein misfolding disease\u201d","volume":"11","author":"Lorenzi","year":"2004","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib14","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1007\/0-387-23226-5_18","article-title":"Amyloid inhibitors and \u03b2-sheet breakers","author":"Soto","year":"2005","journal-title":"J. Alzheim. Dis."},{"key":"10.1016\/j.ejmech.2022.114400_bib15","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1038\/nrd1343","article-title":"Small-molecule inhibitors of protein\u2013protein interactions: progressing towards the dream","volume":"3","author":"Arkin","year":"2004","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2022.114400_bib16","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/S0959-440X(03)00100-3","article-title":"Design strategies for anti-amyloid agents","volume":"13","author":"Mason","year":"2003","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.ejmech.2022.114400_bib17","first-page":"2010","article-title":"CSF biomarkers for Alzheimer's disease diagnosis","author":"Anoop","year":"2010","journal-title":"Int. J. Alzheimer's Dis."},{"key":"10.1016\/j.ejmech.2022.114400_bib18","article-title":"Non-polyphenolic natural inhibitors of amyloid aggregation","author":"Ma","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib19","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1007\/s13311-013-0192-7","article-title":"Natural compounds may open new routes to treatment of amyloid diseases","volume":"10","author":"Bieschke","year":"2013","journal-title":"J. Neurother."},{"key":"10.1016\/j.ejmech.2022.114400_bib20","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep38846","article-title":"Investigating the neuroprotective effects of turmeric extract: structural interactions of \u03b2-amyloid peptide with single curcuminoids","volume":"6","author":"Randino","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2022.114400_bib21","doi-asserted-by":"crossref","first-page":"3998","DOI":"10.1016\/j.ejmech.2010.05.056","article-title":"Effect of flavonoids on the A\u03b2 (25-35)-phospholipid bilayers interaction","volume":"45","author":"Tedeschi","year":"2010","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib22","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1055\/a-1019-9819","article-title":"Natural compounds with anti-BACE1 activity as promising therapeutic drugs for treating Alzheimer\u02bcs disease","volume":"85","author":"Naushad","year":"2019","journal-title":"Planta Med."},{"key":"10.1016\/j.ejmech.2022.114400_bib23","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.4155\/fmc-2016-0006","article-title":"\u03b2-Amyloid-acetylcholine molecular interaction: new role of cholinergic mediators in anti-Alzheimer therapy?","volume":"8","author":"Grimaldi","year":"2016","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib24","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1007\/s10571-017-0555-4","article-title":"Effects of acetylcholine on \u03b2-amyloid-induced cPLA2 activation in the TB neuroectodermal cell line: implications for the pathogenesis of Alzheimer's disease","volume":"38","author":"Polverino","year":"2018","journal-title":"Cell. Mol. Neurobiol."},{"key":"10.1016\/j.ejmech.2022.114400_bib25","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1016\/j.ijbiomac.2019.05.109","article-title":"Protein misfolding, aggregation and mechanism of amyloid cytotoxicity: an overview and therapeutic strategies to inhibit aggregation","volume":"134","author":"Zaman","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ejmech.2022.114400_bib26","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1111\/j.1747-0285.2009.00853.x","article-title":"A new series of 1, 3\u2010dihidro\u2010imidazo [1, 5\u2010c] thiazole\u20105, 7\u2010dione derivatives: synthesis and interaction with a\u03b2 (25\u201035) amyloid peptide","volume":"74","author":"Campiglia","year":"2009","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.ejmech.2022.114400_bib27","first-page":"115","article-title":"Interaction of a \u03b2\u2010sheet breaker peptide with lipid membranes","volume":"16","author":"Vitiello","year":"2010","journal-title":"J. Pept. Sci. Off. Publ. Eur. Pept. Soc."},{"key":"10.1016\/j.ejmech.2022.114400_bib28","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.bbrc.2011.11.061","article-title":"The iA\u03b25p \u03b2-breaker peptide regulates the A\u03b2 (25\u201335) interaction with lipid bilayers through a cholesterol-mediated mechanism","volume":"417","author":"Vitiello","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ejmech.2022.114400_bib29","doi-asserted-by":"crossref","first-page":"3749","DOI":"10.2174\/0929867324666170712161829","article-title":"An overview of new possible treatments of Alzheimer's disease, based on natural products and semi-synthetic compounds","volume":"24","author":"Zanforlin","year":"2017","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib30","doi-asserted-by":"crossref","first-page":"36","DOI":"10.2174\/1874091X01711010036","article-title":"Identification of cysteine ubiquitylation sites on the Sec23A protein of the COPII complex required for vesicle formation from the ER","volume":"11","author":"Amodio","year":"2017","journal-title":"Open Biochem. J."},{"key":"10.1016\/j.ejmech.2022.114400_bib31","doi-asserted-by":"crossref","DOI":"10.1016\/j.ab.2020.113921","article-title":"Development of peptide aptamers as alternatives for antibody in the detection of amyloid-beta 42 aggregates","volume":"609","author":"Kim","year":"2020","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.ejmech.2022.114400_bib32","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1016\/j.tibtech.2011.06.009","article-title":"Molecular aptamers for drug delivery","volume":"29","author":"Tan","year":"2011","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.ejmech.2022.114400_bib33","doi-asserted-by":"crossref","first-page":"3715","DOI":"10.1021\/cr0306743","article-title":"Functional aptamers and aptazymes in biotechnology, diagnostics, and therapy","volume":"107","author":"Famulok","year":"2007","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ejmech.2022.114400_bib34","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/j.cbpa.2006.04.003","article-title":"Nucleic acid aptamers and enzymes as sensors","volume":"10","author":"Navani","year":"2006","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.ejmech.2022.114400_bib35","doi-asserted-by":"crossref","first-page":"3372","DOI":"10.1002\/anie.201906908","article-title":"Peptide\u2010based molecular strategies to interfere with protein misfolding, aggregation, and cell degeneration","volume":"59","author":"Armiento","year":"2020","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.ejmech.2022.114400_bib36","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2020.115676","article-title":"Design and synthesis of \u03b2-strand-fixed peptides inhibiting aggregation of amyloid \u03b2-protein","volume":"28","author":"Tanaka","year":"2020","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib37","doi-asserted-by":"crossref","first-page":"3076","DOI":"10.1039\/D0TB00144A","article-title":"Ferrocene-modified peptides as inhibitors against insulin amyloid aggregation based on molecular simulation","volume":"8","author":"Yao","year":"2020","journal-title":"J. Mater. Chem. B"},{"key":"10.1016\/j.ejmech.2022.114400_bib38","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2020.108614","article-title":"Biophysics, Sequence and structure-based peptides as potent amyloid inhibitors: a review","author":"Mitra","year":"2020","journal-title":"Arch. Biochem."},{"key":"10.1016\/j.ejmech.2022.114400_bib39","doi-asserted-by":"crossref","first-page":"14711","DOI":"10.1002\/ange.201802979","article-title":"Designed macrocyclic peptides as nanomolar amyloid inhibitors based on minimal recognition elements","volume":"130","author":"Spanopoulou","year":"2018","journal-title":"Angew. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib40","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3390\/molecules23020283","article-title":"Peptides as potential therapeutics for Alzheimer's disease","volume":"23","author":"Ribari\u010d","year":"2018","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2022.114400_bib41","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.biopsych.2017.08.010","article-title":"Anti-amyloid-\u03b2 monoclonal antibodies for Alzheimer's disease: pitfalls and promise","volume":"83","author":"van Dyck","year":"2018","journal-title":"Biol. Psychiatr."},{"key":"10.1016\/j.ejmech.2022.114400_bib42","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1016\/j.bmc.2015.02.041","article-title":"\u03b2-sheet interfering molecules acting against \u03b2-amyloid aggregation and fibrillogenesis","volume":"23","author":"Francioso","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib43","doi-asserted-by":"crossref","first-page":"9906","DOI":"10.1021\/bi060837s","article-title":"N-Methylated peptide inhibitors of \u03b2-amyloid aggregation and toxicity. Optimization of the inhibitor structure","volume":"45","author":"Kokkoni","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2022.114400_bib44","doi-asserted-by":"crossref","first-page":"8338","DOI":"10.1021\/bi300415v","article-title":"The N-methylated peptide SEN304 powerfully inhibits A\u03b2 (1\u201342) toxicity by perturbing oligomer formation","volume":"51","author":"Amijee","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2022.114400_bib45","article-title":"Preclinical pharmacokinetic studies of the tritium labelled D-enantiomeric peptide D3 developed for the treatment of Alzheimer s disease","volume":"10","author":"Jiang","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2022.114400_bib46","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.nbd.2009.03.007","article-title":"Oral apolipoprotein AI mimetic peptide improves cognitive function and reduces amyloid burden in a mouse model of Alzheimer's disease","volume":"34","author":"Handattu","year":"2009","journal-title":"Neurobiol. Dis."},{"issue":"5","key":"10.1016\/j.ejmech.2022.114400_bib47","doi-asserted-by":"crossref","DOI":"10.1161\/JAHA.119.014923","article-title":"New nutraceutical combination reduces blood pressure and improves exercise capacity in hypertensive patients via a nitric oxide-dependent mechanism","volume":"9","author":"Carrizzo","year":"2020","journal-title":"J. Am. Heart Assoc."},{"key":"10.1016\/j.ejmech.2022.114400_bib48","doi-asserted-by":"crossref","first-page":"3261","DOI":"10.1021\/bi100144m","article-title":"Development of a proteolytically stable retro-inverso peptide inhibitor of \u03b2-amyloid oligomerization as a potential novel treatment for Alzheimer's disease","volume":"49","author":"Taylor","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2022.114400_bib49","doi-asserted-by":"crossref","first-page":"149","DOI":"10.3233\/JAD-150767","article-title":"Effect of anserine\/carnosine supplementation on verbal episodic memory in elderly people","volume":"50","author":"Hisatsune","year":"2016","journal-title":"Int. J. Alzheimer's Dis."},{"key":"10.1016\/j.ejmech.2022.114400_bib50","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/57e0a947-8600-4658-b04c-cf7a45c8bd8d","article-title":"A novel retro-inverso peptide inhibitor reduces amyloid deposition, oxidation and inflammation and stimulates neurogenesis in the APPswe\/PS1\u0394E9 mouse model of Alzheimer's disease","volume":"8","author":"Parthsarathy","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2022.114400_bib51","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.nano.2016.10.006","article-title":"Retro-inverso peptide inhibitor nanoparticles as potent inhibitors of aggregation of the Alzheimer's A\u03b2 peptide","volume":"13","author":"Gregori","year":"2017","journal-title":"Nanomed. Nanotechnol. Biol. Med."},{"key":"10.1016\/j.ejmech.2022.114400_bib52","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1021\/acschemneuro.6b00006","article-title":"C-terminal fragment, A\u03b232\u201337, analogues protect against a\u03b2 aggregation-induced toxicity","volume":"7","author":"Bansal","year":"2016","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2022.114400_bib53","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/j.npep.2010.03.001","article-title":"A\u03b220\u201329 peptide blocking apoE\/A\u03b2 interaction reduces full-length A\u03b242\/40 fibril formation and cytotoxicity in vitro","volume":"44","author":"Hao","year":"2010","journal-title":"Neuropeptides"},{"key":"10.1016\/j.ejmech.2022.114400_bib54","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1023\/B:MCBI.0000049373.15558.b8","article-title":"Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone","volume":"267","author":"Santhoshkumar","year":"2004","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.ejmech.2022.114400_bib55","doi-asserted-by":"crossref","first-page":"3474","DOI":"10.1021\/ja310064v","article-title":"In vitro and mechanistic studies of an antiamyloidogenic self-assembled cyclic d, l-\u03b1-peptide architecture","volume":"135","author":"Richman","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2022.114400_bib56","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1021\/bi701415b","article-title":"Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's \u03b2-amyloid peptide","volume":"47","author":"Austen","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2022.114400_bib57","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1002\/psc.2784","article-title":"Inhibition of \u03b2\u2010amyloid peptide self\u2010assembly and cytotoxicity by poly (LVFF\u2010co\u2010\u03b2\u2010amino ester)","volume":"21","author":"Xie","year":"2015","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.ejmech.2022.114400_bib58","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/alzrt261","article-title":"Crystal structure reveals conservation of amyloid-\u03b2 conformation recognized by 3D6 following humanization to bapineuzumab","volume":"6","author":"Feinberg","year":"2014","journal-title":"Alzheimer's Res. Ther."},{"key":"10.1016\/j.ejmech.2022.114400_bib59","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-018-24501-0","article-title":"Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-\u03b2","volume":"8","author":"Arndt","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2022.114400_bib60","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.jmb.2011.11.047","article-title":"Structural basis of C-terminal \u03b2-amyloid peptide binding by the antibody ponezumab for the treatment of Alzheimer's disease","volume":"421","author":"La Porte","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ejmech.2022.114400_bib61","doi-asserted-by":"crossref","first-page":"9649","DOI":"10.1038\/srep09649","article-title":"Molecular basis for mid-region amyloid-\u03b2 capture by leading Alzheimer's disease immunotherapies","volume":"5","author":"Crespi","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2022.114400_bib62","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep39374","article-title":"Structure of crenezumab complex with A\u03b2 shows loss of \u03b2-hairpin","volume":"6","author":"Ultsch","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2022.114400_bib63","first-page":"229","article-title":"Fibril aggregation inhibitory activity of the \u03b2\u2010sheet breaker peptides: a molecular docking approach","volume":"15","author":"Chini","year":"2009","journal-title":"J. Pept. Sci. Off. Publ. Eur. Pept. Soc."},{"key":"10.1016\/j.ejmech.2022.114400_bib64","series-title":"Drug Administration FDA Grants Accelerated Approval for Alzheimer's Drug","author":"Food","year":"2021"},{"key":"10.1016\/j.ejmech.2022.114400_bib65","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1750-1326-8-36","article-title":"Immunotherapy for Alzheimer's disease: hoops and hurdles","volume":"8","author":"Lemere","year":"2013","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.ejmech.2022.114400_bib66","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1093\/bib\/bbz095","article-title":"Computational approaches to therapeutic antibody design: established methods and emerging trends","volume":"21","author":"Norman","year":"2020","journal-title":"Briefings Bioinf."},{"key":"10.1016\/j.ejmech.2022.114400_bib67","series-title":"Maestro","author":"Schr\u00f6dinger","year":"2018"},{"key":"10.1016\/j.ejmech.2022.114400_bib68","doi-asserted-by":"crossref","first-page":"2454","DOI":"10.1021\/acs.jcim.1c00410","article-title":"Improving the performance of MM\/PBSA in protein\u2013protein interactions via the screening electrostatic energy","volume":"61","author":"Sheng","year":"2021","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.ejmech.2022.114400_bib69","doi-asserted-by":"crossref","first-page":"E4976","DOI":"10.1073\/pnas.1600749113","article-title":"Atomic-resolution structure of a disease-relevant A\u03b2 (1\u201342) amyloid fibril","volume":"113","author":"W\u00e4lti","year":"2016","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ejmech.2022.114400_bib70","author":"DeLano","year":"2002","journal-title":"The PyMOL Molecular Graphics System, Version 2.0 Schr\u00f6dinger, LLC"},{"key":"10.1016\/j.ejmech.2022.114400_bib71","first-page":"19","volume":"1","author":"Abraham","year":"2015"},{"key":"10.1016\/j.ejmech.2022.114400_bib72","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.1002\/jcc.23354","article-title":"CHARMM36 all\u2010atom additive protein force field: Validation based on comparison to NMR data","volume":"34","author":"Huang","year":"2013","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.ejmech.2022.114400_bib73","series-title":"Microsoft Excel","article-title":"MicrosoftCorporation","year":"2018"},{"key":"10.1016\/j.ejmech.2022.114400_bib74","doi-asserted-by":"crossref","first-page":"1266","DOI":"10.1111\/j.1742-4658.2008.06862.x","article-title":"A facile method for expression and purification of the Alzheimer's disease\u2010associated amyloid \u03b2\u2010peptide","volume":"276","author":"Walsh","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.ejmech.2022.114400_bib75","series-title":"Molecular Cloning, J Decontamination of Dilute Solutions of Ethidium Bromide","author":"Maniatis","year":"1989"},{"key":"10.1016\/j.ejmech.2022.114400_bib76","doi-asserted-by":"crossref","first-page":"240","DOI":"10.3109\/13506129709003835","article-title":"Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid \u03b2-peptide","volume":"4","author":"Jao","year":"1997","journal-title":"Amyloid"},{"key":"10.1016\/j.ejmech.2022.114400_bib77","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1002\/9780470122778.ch6","article-title":"Solid\u2010phase peptide synthesis","volume":"32","author":"Merrifield","year":"1969","journal-title":"Adv. Enzymol. Relat. Area Mol. Biol."},{"key":"10.1016\/j.ejmech.2022.114400_bib78","doi-asserted-by":"crossref","first-page":"W668","DOI":"10.1093\/nar\/gkh371","article-title":"DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data","volume":"32","author":"Whitmore","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ejmech.2022.114400_bib79","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1021\/ed101169t","article-title":"Saturation-transfer difference (STD) NMR: a simple and fast method for ligand screening and characterization of protein binding","volume":"88","author":"Viegas","year":"2011","journal-title":"J. Chem. Educ."},{"key":"10.1016\/j.ejmech.2022.114400_bib80","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pnmrs.2013.02.001","article-title":"Using chemical shift perturbation to characterise ligand binding","volume":"73","author":"Williamson","year":"2013","journal-title":"Prog. Nucl. Magn. Reson. Spectrosc."},{"key":"10.1016\/j.ejmech.2022.114400_bib81","series-title":"SPARKY 3","first-page":"15","author":"Goddard","year":"2004"},{"key":"10.1016\/j.ejmech.2022.114400_bib82","series-title":"Journal of Cellular Biochemistry","article-title":"UCSF Sparky-an NMR display, annotation and assignment tool","author":"Kneller","year":"1993"},{"key":"10.1016\/j.ejmech.2022.114400_bib83","doi-asserted-by":"crossref","first-page":"119","DOI":"10.3109\/13506129.2011.582902","article-title":"The generic amyloid formation inhibition effect of a designed small aromatic \u03b2-breaking peptide","volume":"18","author":"Frydman-Marom","year":"2011","journal-title":"Amyloid"},{"key":"10.1016\/j.ejmech.2022.114400_bib84","doi-asserted-by":"crossref","first-page":"732","DOI":"10.3390\/ph14080732","article-title":"Exploring the early stages of the amyloid a\u03b2 (1\u201342) peptide aggregation process: an NMR study","volume":"14","author":"Santoro","year":"2021","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.ejmech.2022.114400_bib85","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1038\/nature19323","article-title":"The antibody aducanumab reduces A\u03b2 plaques in Alzheimer's disease","volume":"537","author":"Sevigny","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2022.114400_bib86","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1016\/j.bbamem.2009.12.012","article-title":"Membrane charge dependent states of the \u03b2-amyloid fragment A\u03b2 (16\u201335) with differently charged micelle aggregates","volume":"1798","author":"Grimaldi","year":"2010","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.ejmech.2022.114400_bib87","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1051\/epn\/19861701011","article-title":"NMR with proteins and nucleic acids","volume":"17","author":"W\u00fcthrich","year":"1986","journal-title":"EuroPhys. News"},{"key":"10.1016\/j.ejmech.2022.114400_bib88","first-page":"353","article-title":"Automated NMR structure calculation with CYANA","volume":"278","author":"Guntert","year":"2004","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.ejmech.2022.114400_bib89","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1002\/pro.5560050204","article-title":"PROMOTIF\u2014a program to identify and analyze structural motifs in proteins","volume":"5","author":"Hutchinson","year":"1996","journal-title":"Protein Sci."},{"key":"10.1016\/j.ejmech.2022.114400_bib90","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.pep.2011.05.012","article-title":"Expression and purification of 15N-and 13C-isotope labeled 40-residue human Alzheimer's \u03b2-amyloid peptide for NMR-based structural analysis","volume":"79","author":"Long","year":"2011","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.ejmech.2022.114400_bib91","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1002\/pro.3105","article-title":"Pinning down protein interactions by NMR","volume":"26","author":"Teilum","year":"2017","journal-title":"Protein Sci."},{"key":"10.1016\/j.ejmech.2022.114400_bib92","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0115780","article-title":"Aggregation of ass (25-35) on dopc and dopc\/dha bilayers: an atomic force microscopy study","volume":"9","author":"Sublimi Saponetti","year":"2014","journal-title":"J PloS one"},{"key":"10.1016\/j.ejmech.2022.114400_bib93","first-page":"374","article-title":"First-order kinetic model of Alzheimer\u2019s beta-amyloid fibril extension in vitro","volume":"74","author":"Naiki","year":"1996","journal-title":"Lab Invest."},{"key":"10.1016\/j.ejmech.2022.114400_bib94","first-page":"111","volume":"69","author":"Campiglia","year":"2007"},{"key":"10.1016\/j.ejmech.2022.114400_bib95","first-page":"5820","volume":"132","author":"Niu","year":"2020"},{"key":"10.1016\/j.ejmech.2022.114400_bib96","first-page":"672","volume":"226","author":"Soto","year":"1996"},{"key":"10.1016\/j.ejmech.2022.114400_bib97","first-page":"404","volume":"2","author":"Levine","year":"1993"},{"key":"10.1016\/j.ejmech.2022.114400_bib98","series-title":"Methods in Enzymology","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/S0076-6879(99)09020-5","article-title":"[18] Quantification of \u03b2-sheet amyloid fibril structures with thioflavin T","author":"LeVine","year":"1999"},{"key":"10.1016\/j.ejmech.2022.114400_bib99","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1002\/cphc.201701253","article-title":"Investigating protein\u2013ligand interactions by solution nuclear magnetic resonance spectroscopy","volume":"19","author":"Becker","year":"2018","journal-title":"ChemPhysChem"}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523422003026?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523422003026?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T14:44:22Z","timestamp":1759329862000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523422003026"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,7]]},"references-count":99,"alternative-id":["S0223523422003026"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2022.114400","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2022,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"New A\u03b2(1\u201342) ligands from anti-amyloid antibodies: Design, synthesis, and structural interaction","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2022.114400","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"114400"}}