{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T19:06:29Z","timestamp":1790363189241,"version":"4.1.0"},"reference-count":36,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,9,1]],"date-time":"2018-09-01T00:00:00Z","timestamp":1535760000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2018,9]]},"DOI":"10.1016\/j.abb.2018.06.004","type":"journal-article","created":{"date-parts":[[2018,6,13]],"date-time":"2018-06-13T00:22:30Z","timestamp":1528849350000},"page":"1-9","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":15,"special_numbering":"C","title":["Designing a new multifunctional peptide for metal chelation and A\u03b2 inhibition"],"prefix":"10.1016","volume":"653","author":[{"given":"Amir","family":"Shamloo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohsen","family":"Asadbegi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9274-3845","authenticated-orcid":false,"given":"Vahid","family":"Khandan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amirhossein","family":"Amanzadi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"no. 8","key":"10.1016\/j.abb.2018.06.004_bib1","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1016\/j.bmc.2015.02.041","article-title":"beta-sheet interfering molecules acting against beta-amyloid aggregation and fibrillogenesis","volume":"23","author":"Francioso","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"no. 1","key":"10.1016\/j.abb.2018.06.004_bib2","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":"Alzheimers. Dement."},{"issue":"no. 5054","key":"10.1016\/j.abb.2018.06.004_bib3","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1126\/science.1566067","article-title":"Alzheimer's disease: the amyloid cascade hypothesis","volume":"256","author":"Hardy","year":"1992","journal-title":"Science"},{"issue":"no. 1","key":"10.1016\/j.abb.2018.06.004_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2478\/v10007-011-0006-6","article-title":"Metal ions, Alzheimer's disease and chelation therapy","volume":"61","author":"Budimir","year":"2011","journal-title":"Acta Pharm."},{"issue":"no. 30","key":"10.1016\/j.abb.2018.06.004_bib5","doi-asserted-by":"crossref","first-page":"3231","DOI":"10.2174\/138161208786404137","article-title":"Amyloid beta-protein assembly as a therapeutic target of Alzheimer's disease","volume":"14","author":"Yamin","year":"2008","journal-title":"Curr. Pharmaceut. Des."},{"issue":"no. 24","key":"10.1016\/j.abb.2018.06.004_bib6","doi-asserted-by":"crossref","first-page":"8451","DOI":"10.1021\/jm200982p","article-title":"C-terminal tetrapeptides inhibit A\u03b242-induced neurotoxicity primarily through specific interaction at the N-Terminus of A\u03b242","volume":"54","author":"Li","year":"2011","journal-title":"J. Med. Chem."},{"issue":"no. 47","key":"10.1016\/j.abb.2018.06.004_bib7","doi-asserted-by":"crossref","first-page":"29525","DOI":"10.1074\/jbc.271.47.29525","article-title":"A strategy for designing inhibitors of beta-amyloid toxicity","volume":"271","author":"Ghanta","year":"1996","journal-title":"J. Biol. Chem."},{"issue":"no. 15","key":"10.1016\/j.abb.2018.06.004_bib8","doi-asserted-by":"crossref","first-page":"8545","DOI":"10.1074\/jbc.271.15.8545","article-title":"Arrest of beta-amyloid fibril formation by a pentapeptide ligand","volume":"271","author":"Tjernberg","year":"1996","journal-title":"J. Biol. Chem."},{"issue":"no. 16","key":"10.1016\/j.abb.2018.06.004_bib9","doi-asserted-by":"crossref","first-page":"13905","DOI":"10.1074\/jbc.M211976200","article-title":"Pharmacological profiles of peptide drug candidates for the treatment of Alzheimer's disease","volume":"278","author":"Adessi","year":"2003","journal-title":"J. Biol. Chem."},{"issue":"no. 7","key":"10.1016\/j.abb.2018.06.004_bib10","doi-asserted-by":"crossref","first-page":"602","DOI":"10.2174\/156720510793499048","article-title":"Effects of 8-residue beta sheet breaker peptides on aged A\u03b240 \u2013 induced memory impairment and A\u03b240 expression in rat brain and serum following intraamygdaloid injection","volume":"7","author":"Hatip","year":"2010","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.abb.2018.06.004_bib11","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.envres.2017.05.011","article-title":"Cadmium and Alzheimer's disease mortality in U.S. adults: updated evidence with a urinary biomarker and extended follow-up time","volume":"157","author":"Peng","year":"2017","journal-title":"Environ. Res."},{"issue":"no. 3","key":"10.1016\/j.abb.2018.06.004_bib12","doi-asserted-by":"crossref","first-page":"457","DOI":"10.3233\/JAD-2009-1068","article-title":"Challenges associated with metal chelation therapy in Alzheimer's disease","volume":"17","author":"Hegde","year":"2009","journal-title":"J. Alzheimers. Dis."},{"issue":"no. 11","key":"10.1016\/j.abb.2018.06.004_bib13","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1016\/j.bbadis.2012.07.004","article-title":"Na+ and K+ ion imbalances in Alzheimer's disease","volume":"1822","author":"Vitvitsky","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"issue":"no. 1","key":"10.1016\/j.abb.2018.06.004_bib14","doi-asserted-by":"crossref","first-page":"11","DOI":"10.2174\/1389557043487583","article-title":"Chemical and biological considerations in the treatment of metal intoxications by chelating agents","volume":"4","author":"Andersen","year":"2004","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.abb.2018.06.004_bib15","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.foodchem.2014.10.030","article-title":"Affinity purification and characterisation of zinc chelating peptides from rapeseed protein hydrolysates: possible contribution of characteristic amino acid residues","volume":"173","author":"Xie","year":"2015","journal-title":"Food Chem."},{"issue":"no. 16","key":"10.1016\/j.abb.2018.06.004_bib16","doi-asserted-by":"crossref","first-page":"6509","DOI":"10.1021\/jf0712705","article-title":"Affinity purification of copper-chelating peptides from sunflower protein hydrolysates","volume":"55","author":"Meg\u00edas","year":"2007","journal-title":"J. Agric. Food Chem."},{"issue":"no. 2","key":"10.1016\/j.abb.2018.06.004_bib17","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/j.foodchem.2012.02.204","article-title":"Separation and identification of zinc-chelating peptides from sesame protein hydrolysate using IMAC-Zn2+ and LC\u2013MS\/MS","volume":"134","author":"Wang","year":"2012","journal-title":"Food Chem."},{"issue":"no. 5","key":"10.1016\/j.abb.2018.06.004_bib18","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1016\/j.procbio.2013.04.013","article-title":"Preparation, isolation and identification of iron-chelating peptides derived from Alaska pollock skin","volume":"48","author":"Guo","year":"2013","journal-title":"Process Biochem."},{"issue":"no. 1","key":"10.1016\/j.abb.2018.06.004_bib19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0022-510X(01)00672-4","article-title":"Determination of cadmium and zinc in Alzheimer's brain tissue using inductively coupled plasma mass spectrometry","volume":"195","author":"Panayi","year":"2002","journal-title":"J. Neurol. Sci."},{"issue":"no. 2","key":"10.1016\/j.abb.2018.06.004_bib20","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1007\/s10534-014-9719-6","article-title":"Heavy metals toxicity: effect of cadmium ions on amyloid beta protein 1-42. Possible implications for Alzheimer's disease","volume":"27","author":"Notarachille","year":"2014","journal-title":"Biometals"},{"issue":"no. 13","key":"10.1016\/j.abb.2018.06.004_bib21","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2013a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"issue":"no. 3","key":"10.1016\/j.abb.2018.06.004_bib22","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1021\/ct700301q","article-title":"GROMACS 4:\u2009 algorithms for highly efficient, load-balanced, and scalable molecular simulation","volume":"4","author":"Hess","year":"2008","journal-title":"J. Chem. Theor. Comput."},{"issue":"no. 11","key":"10.1016\/j.abb.2018.06.004_bib23","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1021\/cn300091a","article-title":"The role of molecular simulations in the development of inhibitors of amyloid beta-peptide aggregation for the treatment of Alzheimer's disease","volume":"3","author":"Lemkul","year":"2012","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.abb.2018.06.004_bib24","doi-asserted-by":"crossref","first-page":"W363","DOI":"10.1093\/nar\/gki481","article-title":"PatchDock and SymmDock: servers for rigid and symmetric docking","volume":"33","author":"Schneidman-Duhovny","year":"2005","journal-title":"Nucleic Acids Res."},{"issue":"no. 1","key":"10.1016\/j.abb.2018.06.004_bib25","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1002\/prot.21495","article-title":"FireDock: fast interaction refinement in molecular docking","volume":"69","author":"Andrusier","year":"2007","journal-title":"Proteins"},{"key":"10.1016\/j.abb.2018.06.004_bib26","doi-asserted-by":"crossref","first-page":"W229","DOI":"10.1093\/nar\/gkn186","article-title":"FireDock: a web server for fast interaction refinement in molecular docking","volume":"36","author":"Mashiach","year":"2008","journal-title":"Nucleic Acids Res."},{"issue":"no. 4","key":"10.1016\/j.abb.2018.06.004_bib27","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1002\/jcc.21367","article-title":"CHARMM general force field: a force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields","volume":"31","author":"Vanommeslaeghe","year":"2010","journal-title":"J. Comput. Chem."},{"issue":"no. 1","key":"10.1016\/j.abb.2018.06.004_bib28","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S0166-1280(96)04874-9","article-title":"A quantum-mechanical study of metal binding sites in zinc finger structures","volume":"423","author":"Topol","year":"1998","journal-title":"J. Mol. Struct. Theochem"},{"issue":"no. 1","key":"10.1016\/j.abb.2018.06.004_bib29","doi-asserted-by":"crossref","first-page":"33","DOI":"10.2174\/156802610790232242","article-title":"Quantum mechanical methods for drug design","volume":"10","author":"Zhou","year":"2010","journal-title":"Curr. Top. Med. Chem."},{"issue":"no. 29","key":"10.1016\/j.abb.2018.06.004_bib30","doi-asserted-by":"crossref","first-page":"2524","DOI":"10.1002\/jcc.23416","article-title":"Characterization of the polymorphic states of copper(II)-bound A\u03b2(1\u201316) peptides by computational simulations","volume":"34","author":"Xu","year":"2013","journal-title":"J. Comput. Chem."},{"issue":"no. 3","key":"10.1016\/j.abb.2018.06.004_bib31","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/S0009-2614(99)01082-9","article-title":"Gaussian-3 theory: a variation based on third-order perturbation theory and an assessment of the contribution of core-related correlation","volume":"313","author":"Curtiss","year":"1999","journal-title":"Chem. Phys. Lett."},{"issue":"no. 10","key":"10.1016\/j.abb.2018.06.004_bib32","doi-asserted-by":"crossref","first-page":"L84","DOI":"10.1016\/j.bpj.2010.09.015","article-title":"Minimal Zn(2+) binding site of amyloid-\u03b2","volume":"99","author":"Tsvetkov","year":"2010","journal-title":"Biophys. J."},{"issue":"7","key":"10.1016\/j.abb.2018.06.004_bib33","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1016\/j.jbiomech.2015.03.007","article-title":"A viscoelastic model for axonal microtubule rupture","volume":"48","author":"Shamloo","year":"2015","journal-title":"J. Biomech."},{"key":"10.1016\/j.abb.2018.06.004_bib34","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.jbiotec.2015.08.005","article-title":"Integrative utilization of microenvironments, biomaterials and computational techniques for advanced tissue engineering","volume":"212","author":"Shamloo","year":"2015","journal-title":"J. Biotechnol."},{"issue":"3","key":"10.1016\/j.abb.2018.06.004_bib35","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1002\/cm.21429","article-title":"Nanomechanics of actin filament: a molecular dynamics simulation","volume":"75","author":"Shamloo","year":"2017","journal-title":"Cytoskeleton"},{"issue":"6","key":"10.1016\/j.abb.2018.06.004_bib36","doi-asserted-by":"crossref","first-page":"066023","DOI":"10.1088\/1478-3975\/12\/6\/066023","article-title":"A model for cell density effect on stress fiber alignment and collective directional migration","volume":"12","author":"Abeddoust","year":"2015","journal-title":"Phys. Biol."}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986118301097?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986118301097?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,7,7]],"date-time":"2024-07-07T12:40:38Z","timestamp":1720356038000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003986118301097"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,9]]},"references-count":36,"alternative-id":["S0003986118301097"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2018.06.004","relation":{},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2018,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Designing a new multifunctional peptide for metal chelation and A\u03b2 inhibition","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2018.06.004","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}