{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T04:12:22Z","timestamp":1790741542970,"version":"4.1.0"},"reference-count":74,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,12,1]],"date-time":"2024-12-01T00:00:00Z","timestamp":1733011200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"NSFC","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Colloids and Surfaces B: Biointerfaces"],"published-print":{"date-parts":[[2024,12]]},"DOI":"10.1016\/j.colsurfb.2024.114192","type":"journal-article","created":{"date-parts":[[2024,8,30]],"date-time":"2024-08-30T17:32:35Z","timestamp":1725039155000},"page":"114192","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Computational insights into the aggregation mechanism and amyloidogenic core of aortic amyloid medin polypeptide"],"prefix":"10.1016","volume":"244","author":[{"given":"Fengjuan","family":"Huang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiajia","family":"Yan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaohan","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huan","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiangfang","family":"Lian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xi","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chuang","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Feng","family":"Ding","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9799-7131","authenticated-orcid":false,"given":"Yunxiang","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.colsurfb.2024.114192_bib1","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41580-018-0060-8","article-title":"A new era for understanding amyloid structures and disease","volume":"19","author":"Iadanza","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.colsurfb.2024.114192_bib2","doi-asserted-by":"crossref","first-page":"6492","DOI":"10.1039\/C7CS00372B","article-title":"Implications of peptide assemblies in amyloid diseases","volume":"46","author":"Ke","year":"2017","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.colsurfb.2024.114192_bib3","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1021\/acs.chemrev.0c01122","article-title":"Amyloid Oligomers: a joint experimental\/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis","volume":"121","author":"Nguyen","year":"2021","journal-title":"Chem. Rev."},{"key":"10.1016\/j.colsurfb.2024.114192_bib4","doi-asserted-by":"crossref","DOI":"10.1016\/j.nantod.2021.101125","article-title":"Spontaneous formation of beta-sheet nano-barrels during the early aggregation of Alzheimer's amyloid beta","volume":"38","author":"Sun","year":"2021","journal-title":"Nano Today"},{"key":"10.1016\/j.colsurfb.2024.114192_bib5","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.bbadis.2018.11.021","article-title":"Nucleation of beta-rich oligomers and beta-barrels in the early aggregation of human islet amyloid polypeptide","volume":"1865","author":"Sun","year":"2019","journal-title":"Biochim Biophys. Acta Mol. Basis Dis."},{"key":"10.1016\/j.colsurfb.2024.114192_bib6","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1016\/j.bbrc.2007.06.187","article-title":"Unwinding fibril formation of medin, the peptide of the most common form of human amyloid","volume":"361","author":"Larsson","year":"2007","journal-title":"Biochem Biophys. Res Commun."},{"key":"10.1016\/j.colsurfb.2024.114192_bib7","doi-asserted-by":"crossref","first-page":"23925","DOI":"10.1073\/pnas.2011133117","article-title":"Medin aggregation causes cerebrovascular dysfunction in aging wild-type mice","volume":"117","author":"Degenhardt","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.colsurfb.2024.114192_bib8","doi-asserted-by":"crossref","first-page":"2363","DOI":"10.1016\/j.bpj.2015.10.034","article-title":"Oxidative stress alters the morphology and toxicity of aortic medial amyloid","volume":"109","author":"Davies","year":"2015","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2024.114192_bib9","doi-asserted-by":"crossref","first-page":"65","DOI":"10.3389\/fncel.2015.00065","article-title":"Role of amyloid peptides in vascular dysfunction and platelet dysregulation in Alzheimer's disease","volume":"9","author":"Canobbio","year":"2015","journal-title":"Front Cell Neurosci."},{"key":"10.1016\/j.colsurfb.2024.114192_bib10","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1038\/nchem.1433","article-title":"Amyloid beta-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity","volume":"4","author":"Cheng","year":"2012","journal-title":"Nat. Chem."},{"key":"10.1016\/j.colsurfb.2024.114192_bib11","doi-asserted-by":"crossref","first-page":"5004","DOI":"10.1038\/s41467-022-32688-0","article-title":"Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly","volume":"13","author":"Tas","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.colsurfb.2024.114192_bib12","doi-asserted-by":"crossref","first-page":"3918","DOI":"10.1111\/j.1742-4658.2011.08298.x","article-title":"Localized amyloids important in diseases outside the brain-lessons from the islets of Langerhans and the thoracic aorta","volume":"278","author":"Westermark","year":"2011","journal-title":"FEBS J."},{"key":"10.1016\/j.colsurfb.2024.114192_bib13","doi-asserted-by":"crossref","DOI":"10.1016\/j.arr.2020.101176","article-title":"Roles and mechanisms of MFG-E8 in vascular aging-related diseases","volume":"64","author":"Ni","year":"2020","journal-title":"Ageing Res Rev."},{"key":"10.1016\/j.colsurfb.2024.114192_bib14","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.neurobiolaging.2015.09.008","article-title":"Age-related changes in pial arterial structure and blood flow in mice","volume":"37","author":"Kang","year":"2016","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.colsurfb.2024.114192_bib15","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1080\/13506120500107006","article-title":"Medin-amyloid: a recently characterized age-associated arterial amyloid form affects mainly arteries in the upper part of the body","volume":"12","author":"Peng","year":"2005","journal-title":"Amyloid"},{"key":"10.1016\/j.colsurfb.2024.114192_bib16","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1080\/13506120600722530","article-title":"Lactadherin binds to elastin--a starting point for medin amyloid formation?","volume":"13","author":"Larsson","year":"2006","journal-title":"Amyloid"},{"key":"10.1016\/j.colsurfb.2024.114192_bib17","doi-asserted-by":"crossref","first-page":"2429","DOI":"10.1002\/pmic.200800658","article-title":"Comparative proteomic analysis of rat aorta in a subtotal nephrectomy model","volume":"10","author":"Lin","year":"2010","journal-title":"Proteomics"},{"key":"10.1016\/j.colsurfb.2024.114192_bib18","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1126\/science.1213151","article-title":"Atomic view of a toxic amyloid small oligomer","volume":"335","author":"Laganowsky","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.colsurfb.2024.114192_bib19","doi-asserted-by":"crossref","first-page":"2769","DOI":"10.1016\/j.bpj.2020.04.026","article-title":"Medin oligomer membrane pore formation: a potential mechanism of vascular dysfunction","volume":"118","author":"Younger","year":"2020","journal-title":"Biophys. J."},{"key":"10.1016\/j.colsurfb.2024.114192_bib20","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1038\/s43587-023-00481-3","article-title":"Medin amyloid may drive arterial aging and disease in the periphery and brain","volume":"3","author":"Madine","year":"2023","journal-title":"Nat. Aging"},{"key":"10.1016\/j.colsurfb.2024.114192_bib21","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.4103\/1673-5374.387995","article-title":"Medin synergized with vascular amyloid-beta deposits accelerates cognitive decline in Alzheimer's disease: a potential biomarker","volume":"19","author":"Ge","year":"2024","journal-title":"Neural Regen. Res"},{"key":"10.1016\/j.colsurfb.2024.114192_bib22","doi-asserted-by":"crossref","first-page":"229","DOI":"10.3109\/13506129.2011.630761","article-title":"Signs of cross-seeding: aortic medin amyloid as a trigger for protein AA deposition","volume":"18","author":"Larsson","year":"2011","journal-title":"Amyloid"},{"key":"10.1016\/j.colsurfb.2024.114192_bib23","article-title":"Computational insights into the cross-talk between medin and Abeta: implications for age-related vascular risk factors in Alzheimer's disease, Brief Bioinform","volume":"25","author":"Huang","year":"2024"},{"key":"10.1016\/j.colsurfb.2024.114192_bib24","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1038\/s41586-022-05440-3","article-title":"Medin co-aggregates with vascular amyloid-beta in Alzheimer's disease","volume":"612","author":"Wagner","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.colsurfb.2024.114192_bib25","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.pep.2014.02.009","article-title":"Expression and purification of the aortic amyloid polypeptide medin","volume":"98","author":"Davies","year":"2014","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.colsurfb.2024.114192_bib26","doi-asserted-by":"crossref","first-page":"7791","DOI":"10.1074\/jbc.M114.602177","article-title":"Comparisons with amyloid-beta reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin","volume":"290","author":"Davies","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.colsurfb.2024.114192_bib27","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.jmb.2007.08.064","article-title":"Negatively charged phospholipid membranes induce amyloid formation of medin via an alpha-helical intermediate","volume":"374","author":"Olofsson","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114192_bib28","doi-asserted-by":"crossref","first-page":"45224","DOI":"10.1038\/srep45224","article-title":"Probing medin monomer structure and its amyloid nucleation using (13)C-direct detection NMR in combination with structural bioinformatics","volume":"7","author":"Davies","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.colsurfb.2024.114192_bib29","doi-asserted-by":"crossref","first-page":"3089","DOI":"10.1021\/bi802164e","article-title":"Cross-beta spine architecture of fibrils formed by the amyloidogenic segment NFGSVQFV of medin from solid-state NMR and X-ray fiber diffraction measurements","volume":"48","author":"Madine","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2024.114192_bib30","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1080\/13506120412331272287","article-title":"Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments","volume":"11","author":"Reches","year":"2004","journal-title":"Amyloid"},{"key":"10.1016\/j.colsurfb.2024.114192_bib31","doi-asserted-by":"crossref","first-page":"15870","DOI":"10.1021\/jacs.0c06143","article-title":"Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from Medin(19-36)","volume":"142","author":"Howitz","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.colsurfb.2024.114192_bib32","doi-asserted-by":"crossref","first-page":"6376","DOI":"10.1021\/acs.jcim.3c01267","article-title":"Unveiling medin folding and dimerization dynamics and conformations via atomistic discrete molecular dynamics simulations","volume":"63","author":"Huang","year":"2023","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.colsurfb.2024.114192_bib33","doi-asserted-by":"crossref","first-page":"3081","DOI":"10.1002\/anie.200904902","article-title":"Identification of hot regions of the Abeta-IAPP interaction interface as high-affinity binding sites in both cross- and self-association","volume":"49","author":"Andreetto","year":"2010","journal-title":"Angew. Chem. Int Ed. Engl."},{"key":"10.1016\/j.colsurfb.2024.114192_bib34","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.1016\/j.str.2008.03.013","article-title":"Ab initio folding of proteins with all-atom discrete molecular dynamics","volume":"16","author":"Ding","year":"2008","journal-title":"Structure"},{"key":"10.1016\/j.colsurfb.2024.114192_bib35","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1016\/S0076-6879(06)12019-4","article-title":"Ab initio discrete molecular dynamics approach to protein folding and aggregation","volume":"412","author":"Urbanc","year":"2006","journal-title":"Methods Enzym."},{"key":"10.1016\/j.colsurfb.2024.114192_bib36","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.1021\/ci8001167","article-title":"MedusaScore: an accurate force field-based scoring function for virtual drug screening","volume":"48","author":"Yin","year":"2008","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.colsurfb.2024.114192_bib37","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/0076-6879(95)46019-5","article-title":"Raman spectroscopy of DNA and proteins","volume":"246","author":"Peticolas","year":"1995","journal-title":"Methods Enzym."},{"key":"10.1016\/j.colsurfb.2024.114192_bib38","doi-asserted-by":"crossref","first-page":"8375","DOI":"10.1021\/jp2114576","article-title":"Discrete molecular dynamics: an efficient and versatile simulation method for fine protein characterization","volume":"116","author":"Shirvanyants","year":"2012","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.colsurfb.2024.114192_bib39","doi-asserted-by":"crossref","first-page":"10138","DOI":"10.1021\/acs.jpcb.0c07256","article-title":"alphaB-Crystallin chaperone inhibits abeta aggregation by capping the beta-sheet-rich oligomers and fibrils","volume":"124","author":"Sun","year":"2020","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.colsurfb.2024.114192_bib40","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1002\/jcc.540040211","article-title":"Charmm - a program for macromolecular energy, minimization, and dynamics calculations","volume":"4","author":"Brooks","year":"1983","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.colsurfb.2024.114192_bib41","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0959-440X(00)00063-4","article-title":"Effective energy functions for protein structure prediction","volume":"10","author":"Lazaridis","year":"2000","journal-title":"Curr. Opin. Struc Biol."},{"key":"10.1016\/j.colsurfb.2024.114192_bib42","doi-asserted-by":"crossref","first-page":"2056","DOI":"10.1063\/1.472046","article-title":"A Debye-Huckel theory for electrostatic interactions in proteins","volume":"105","author":"Ullner","year":"1996","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.colsurfb.2024.114192_bib43","doi-asserted-by":"crossref","first-page":"3724","DOI":"10.1038\/s41467-018-06133-0","article-title":"Identifying weak interdomain interactions that stabilize the supertertiary structure of the N-terminal tandem PDZ domains of PSD-95","volume":"9","author":"Yanez Orozco","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.colsurfb.2024.114192_bib44","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.77242","article-title":"Fuzzy supertertiary interactions within PSD-95 enable ligand binding","volume":"11","author":"Hamilton","year":"2022","journal-title":"Elife"},{"key":"10.1016\/j.colsurfb.2024.114192_bib45","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1021\/acs.jcim.2c01202","article-title":"Structural perturbation of monomers determines the amyloid aggregation propensity of calcitonin variants","volume":"63","author":"Liu","year":"2023","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.colsurfb.2024.114192_bib46","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1039\/D3SM01332D","article-title":"Deciphering the influence of Y12L and N17H substitutions on the conformation and oligomerization of human calcitonin","volume":"20","author":"Yan","year":"2024","journal-title":"Soft Matter"},{"key":"10.1016\/j.colsurfb.2024.114192_bib47","doi-asserted-by":"crossref","first-page":"4500","DOI":"10.1021\/acs.jcim.4c00553","article-title":"Molecular insights into the effects of F16L and F19L substitutions on the conformation and aggregation dynamics of human calcitonin","volume":"64","author":"Huang","year":"2024","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.colsurfb.2024.114192_bib48","doi-asserted-by":"crossref","first-page":"21773","DOI":"10.1039\/D2CP02851D","article-title":"Molecular insights into the oligomerization dynamics and conformations of amyloidogenic and non-amyloidogenic amylin from discrete molecular dynamics simulations","volume":"24","author":"Wang","year":"2022","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.colsurfb.2024.114192_bib49","article-title":"Molecular insights into the self-assembly of block copolymer suckerin polypeptides into nanoconfined beta-sheets","volume":"18","author":"Liu","year":"2022","journal-title":"Small"},{"key":"10.1016\/j.colsurfb.2024.114192_bib50","doi-asserted-by":"crossref","first-page":"3591","DOI":"10.1021\/acs.jcim.3c00533","article-title":"Dissecting the self-assembly dynamics of imperfect repeats in alpha-synuclein","volume":"63","author":"Huang","year":"2023","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.colsurfb.2024.114192_bib51","doi-asserted-by":"crossref","first-page":"31604","DOI":"10.1039\/D3CP04138G","article-title":"Co-aggregation of alpha-synuclein with amyloid-beta stabilizes beta-sheet-rich oligomers and enhances the formation of beta-barrels","volume":"25","author":"Huang","year":"2023","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.colsurfb.2024.114192_bib52","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.1021\/acs.jctc.6b01153","article-title":"Discrete molecular dynamics approach to the study of disordered and aggregating proteins","volume":"13","author":"Emperador","year":"2017","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.colsurfb.2024.114192_bib53","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abf7668","article-title":"De novo design of peptides that coassemble into beta sheet-based nanofibrils","volume":"7","author":"Xiao","year":"2021","journal-title":"Sci. Adv."},{"key":"10.1016\/j.colsurfb.2024.114192_bib54","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.1700479","article-title":"Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations","volume":"3","author":"Brodie","year":"2017","journal-title":"Sci. Adv."},{"key":"10.1016\/j.colsurfb.2024.114192_bib55","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.str.2023.01.011","article-title":"Structural and dynamic insights into alpha-synuclein dimer conformations","volume":"31","author":"Zamel","year":"2023","journal-title":"Structure"},{"key":"10.1016\/j.colsurfb.2024.114192_bib56","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure - pattern-recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.colsurfb.2024.114192_bib57","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ijbiomac.2021.10.103","article-title":"Hydroxylated single-walled carbon nanotube inhibits beta2m(21)(-)(31) fibrillization and disrupts pre-formed proto-fibrils","volume":"193","author":"Zhang","year":"2021","journal-title":"Int J. Biol. Macromol."},{"key":"10.1016\/j.colsurfb.2024.114192_bib58","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1021\/acs.jcim.0c01319","article-title":"Direct observation of beta-barrel intermediates in the self-assembly of toxic SOD1(28-38) and absence in nontoxic glycine mutants","volume":"61","author":"Sun","year":"2021","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.colsurfb.2024.114192_bib59","doi-asserted-by":"crossref","first-page":"6118","DOI":"10.1021\/acs.jcim.2c00961","article-title":"Decoding the identification mechanism of an SAM-III riboswitch on ligands through multiple independent gaussian-accelerated molecular dynamics simulations","volume":"62","author":"Chen","year":"2022","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.colsurfb.2024.114192_bib60","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1002\/(SICI)1521-3773(19990115)38:1\/2<236::AID-ANIE236>3.0.CO;2-M","article-title":"Peptide folding: when simulation meets experiment","volume":"38","author":"Daura","year":"1999","journal-title":"Angew. Chem. Int Ed."},{"key":"10.1016\/j.colsurfb.2024.114192_bib61","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1007\/s00249-010-0581-3","article-title":"Comparison of aggregation enhancement and inhibition as strategies for reducing the cytotoxicity of the aortic amyloid polypeptide medin","volume":"39","author":"Madine","year":"2010","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.colsurfb.2024.114192_bib62","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1021\/bi020429y","article-title":"The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation","volume":"42","author":"Kessler","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.colsurfb.2024.114192_bib63","doi-asserted-by":"crossref","first-page":"3126","DOI":"10.1021\/acschemneuro.2c00531","article-title":"Molecular insights into the misfolding and dimerization dynamics of the full-length alpha-synuclein from atomistic discrete molecular dynamics simulations","volume":"13","author":"Zhang","year":"2022","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.colsurfb.2024.114192_bib64","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1021\/acschemneuro.8b00537","article-title":"Norepinephrine inhibits Alzheimer's amyloid-beta peptide aggregation and destabilizes amyloid-beta protofibrils: a molecular dynamics simulation study","volume":"10","author":"Zou","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.colsurfb.2024.114192_bib65","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1126\/science.aao2825","article-title":"Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy","volume":"358","author":"Gremer","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.colsurfb.2024.114192_bib66","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1038\/s41594-021-00646-x","article-title":"Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores","volume":"28","author":"Cao","year":"2021","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114192_bib67","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/nsmb.3194","article-title":"Solid-state NMR structure of a pathogenic fibril of full-length human alpha-synuclein","volume":"23","author":"Tuttle","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114192_bib68","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0896-6273(01)00462-7","article-title":"beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor","volume":"32","author":"Hashimoto","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.colsurfb.2024.114192_bib69","doi-asserted-by":"crossref","first-page":"3567","DOI":"10.1021\/acs.jcim.3c00414","article-title":"SEVI inhibits abeta amyloid aggregation by capping the beta-sheet elongation edges","volume":"63","author":"Wang","year":"2023","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.colsurfb.2024.114192_bib70","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/s42003-022-03343-7","article-title":"Cross-seeding between Abeta and SEVI indicates a pathogenic link and gender difference between alzheimer diseases and AIDS","volume":"5","author":"Tang","year":"2022","journal-title":"Commun. Biol."},{"key":"10.1016\/j.colsurfb.2024.114192_bib71","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1038\/nsmb.3108","article-title":"The chaperone alphaB-crystallin uses different interfaces to capture an amorphous and an amyloid client","volume":"22","author":"Mainz","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.colsurfb.2024.114192_bib72","doi-asserted-by":"crossref","first-page":"7398","DOI":"10.1021\/jp300389g","article-title":"Template induced conformational change of amyloid-beta monomer","volume":"116","author":"Xi","year":"2012","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.colsurfb.2024.114192_bib73","doi-asserted-by":"crossref","first-page":"5303","DOI":"10.1021\/acs.jcim.4c00859","article-title":"Computational investigation of coaggregation and cross-seeding between abeta and hIAPP underpinning the cross-talk in Alzheimer's disease and type 2 diabetes","volume":"64","author":"Fan","year":"2024","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.colsurfb.2024.114192_bib74","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.1073\/pnas.052706099","article-title":"Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation","volume":"99","author":"Richardson","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Colloids and Surfaces B: Biointerfaces"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S092777652400451X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S092777652400451X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,9,14]],"date-time":"2024-09-14T18:23:10Z","timestamp":1726338190000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S092777652400451X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,12]]},"references-count":74,"alternative-id":["S092777652400451X"],"URL":"https:\/\/doi.org\/10.1016\/j.colsurfb.2024.114192","relation":{},"ISSN":["0927-7765"],"issn-type":[{"value":"0927-7765","type":"print"}],"subject":[],"published":{"date-parts":[[2024,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Computational insights into the aggregation mechanism and amyloidogenic core of aortic amyloid medin polypeptide","name":"articletitle","label":"Article Title"},{"value":"Colloids and Surfaces B: Biointerfaces","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.colsurfb.2024.114192","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"114192"}}