{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,23]],"date-time":"2026-03-23T12:10:06Z","timestamp":1774267806614,"version":"3.50.1"},"reference-count":0,"publisher":"Bentham Science Publishers Ltd.","issue":"33","content-domain":{"domain":["eurekaselect.com"],"crossmark-restriction":true},"short-container-title":["CMC"],"published-print":{"date-parts":[[2018,10,24]]},"abstract":"<jats:sec>\n<jats:title\/>\n<jats:p>Alzheimer\u2019s disease (AD) is a widespread form of dementia that is estimated to\naffect 44.4 million people worldwide. AD pathology is closely related to the accumulation of\namyloid beta (A\u03b2) peptides in fibrils and plagues, the small oligomeric intermediate species\nformed during the A\u03b2 peptides aggregation presenting the highest neurotoxicity.\n<\/jats:p><\/jats:sec>\n<jats:sec>\n<jats:title\/>\n<jats:p>\nThis review discusses the recent advances on the A\u03b2 peptides electrochemical\ncharacterization. The A\u03b2 peptides oxidation at a glassy carbon electrode occurs in one or two\nsteps, depending on the amino acid sequence, length and content. The first electron transfer\nreaction corresponds to the tyrosine Tyr10 amino acid residue oxidation, and the second to all\nthree histidine (His6, His13 and His14) and one methionine (Met35) amino acid residues. The\nA\u03b2 peptides aggregation and amyloid fibril formation are electrochemically detected via the\nelectroactive amino acids oxidation peak currents decrease that occurs in a time dependent\nmanner. The A\u03b2 peptides redox behaviour is correlated with changes in the adsorption\nmorphology from initially random coiled structures, corresponding to the A\u03b2 peptide\nmonomers in random coil or in \u03b1-helix conformations, to aggregates, protofibrils and two\ntypes of fibrils, corresponding to the A\u03b2 peptides in a \u03b2-sheet configuration, observed by\natomic force microscopy. Electrochemical studies of A\u03b2 peptides aggregation, mediated by\nthe interaction with metal ions, particularly zinc, copper and iron, and different methodologies\nconcerning the detection of A\u03b2 peptide biomarkers of AD in biological fluids, using\nelectrochemical biosensors, are also discussed.<\/jats:p>\n<\/jats:sec>","DOI":"10.2174\/0929867325666180214112536","type":"journal-article","created":{"date-parts":[[2018,2,17]],"date-time":"2018-02-17T06:27:12Z","timestamp":1518848832000},"page":"4066-4083","update-policy":"https:\/\/doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Electrochemistry of Alzheimer Disease Amyloid Beta Peptides"],"prefix":"10.2174","volume":"25","author":[{"given":"Ana-Maria","family":"Chiorcea-Paquim","sequence":"first","affiliation":[{"name":"Department of Chemistry, Faculty of Sciences and Technology, University of Coimbra, 3004-535, Coimbra, Portugal"}]},{"given":"Teodor Adrian","family":"Enache","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Sciences and Technology, University of Coimbra, 3004-535, Coimbra, Portugal"}]},{"given":"Ana Maria","family":"Oliveira-Brett","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Sciences and Technology, University of Coimbra, 3004-535, Coimbra, Portugal"}]}],"member":"965","container-title":["Current Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/eurekaselect.com\/article\/download\/159826","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.eurekaselect.com\/159826\/article","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/eurekaselect.com\/article\/download\/159826","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,12,25]],"date-time":"2020-12-25T09:49:25Z","timestamp":1608889765000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.eurekaselect.com\/159826\/article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,10,24]]},"references-count":0,"journal-issue":{"issue":"33","published-print":{"date-parts":[[2018,10,24]]}},"alternative-id":["LiveAll1"],"URL":"https:\/\/doi.org\/10.2174\/0929867325666180214112536","relation":{},"ISSN":["0929-8673"],"issn-type":[{"value":"0929-8673","type":"print"}],"subject":[],"published":{"date-parts":[[2018,10,24]]},"assertion":[{"value":"Peer Reviewed","order":0,"name":"review_status","label":"Review Status","group":{"name":"peer_review_details","label":"Peer Review Details"}},{"value":"Single blind","order":1,"name":"review_process","label":"Review Process","group":{"name":"peer_review_details","label":"Peer Review Details"}},{"value":"Checked with iThenticate","order":0,"name":"screening_status","label":"Screening Status","group":{"name":"plagiarism_screening","label":"Plagiarism Screening"}},{"value":"2017-03-14","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2017-05-18","order":1,"name":"revised","label":"Revised","group":{"name":"publication_history","label":"Publication History"}},{"value":"2017-05-18","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2018-10-24","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}