{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,26]],"date-time":"2026-03-26T16:34:15Z","timestamp":1774542855131,"version":"3.50.1"},"reference-count":104,"publisher":"IOP Publishing","issue":"3","license":[{"start":{"date-parts":[[2025,7,17]],"date-time":"2025-07-17T00:00:00Z","timestamp":1752710400000},"content-version":"vor","delay-in-days":16,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2025,7,17]],"date-time":"2025-07-17T00:00:00Z","timestamp":1752710400000},"content-version":"tdm","delay-in-days":16,"URL":"https:\/\/iopscience.iop.org\/info\/page\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council","doi-asserted-by":"crossref","award":["2024-06426"],"award-info":[{"award-number":["2024-06426"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100006054","name":"University of Guanajuato","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100006054","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"crossref","award":["38496"],"award-info":[{"award-number":["38496"]}],"id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Mexico\u2019s National Council of Humanities, Sciences, and Technologies","award":["A1-S-29906"],"award-info":[{"award-number":["A1-S-29906"]}]}],"content-domain":{"domain":["iopscience.iop.org"],"crossmark-restriction":false},"short-container-title":["Prog. Biomed. Eng."],"published-print":{"date-parts":[[2025,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Transcranial stimulation has emerged as a non-invasive treatment that applies electrical currents and magnetic fields to regulate brain functions. Previous studies have shown that magnetic stimulation modulates the dynamics of charged molecules in biological systems. In some pathologies, once the electrical or magnetic field is applied directly to subjects, it can interact with, and alter, abnormally folded proteins, including amyloid-<jats:italic>\u03b2<\/jats:italic> peptides and their aggregates, reducing cognitive impairments. While our understanding of the molecular mechanisms underlying the interaction between amyloid-<jats:italic>\u03b2<\/jats:italic> peptide and the physical forces generated by electrical or magnetic stimulation remains unclear, observations show that these stimuli exert attractive and repulsive forces while interacting with the charged groups of peptide side chains as well as lipids. These interactions influence hydrophobic packing and secondary structure, ultimately inducing alterations in aggregation kinetics. The study of structural models of amyloidogenic proteins aids in understanding the mechanisms involved in the protein aggregation process and suggests possible therapeutic applications. This review examines proposed molecular mechanisms to explain the modulatory effects of external electromagnetic fields on the dynamics of proteins and their complexes that regulate pathological processes associated with amyloid-<jats:italic>\u03b2<\/jats:italic> peptide fibrillation.<\/jats:p>","DOI":"10.1088\/2516-1091\/adea02","type":"journal-article","created":{"date-parts":[[2025,6,30]],"date-time":"2025-06-30T18:54:22Z","timestamp":1751309662000},"page":"032010","update-policy":"https:\/\/doi.org\/10.1088\/crossmark-policy","source":"Crossref","is-referenced-by-count":1,"title":["Molecular mechanisms associated with the interaction of external electromagnetic fields in protein dynamics and aggregation: a focus on amyloid-<i>\u03b2<\/i> peptide"],"prefix":"10.1088","volume":"7","author":[{"given":"Maldonado-Moreles","family":"Alejandro","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bonilla-Jaime","family":"Herlinda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0036-7227","authenticated-orcid":true,"given":"Diana I","family":"Aparicio-Bautista","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1335-226X","authenticated-orcid":true,"given":"Mondrag\u00f3n-Rodr\u00edguez","family":"Siddhartha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3114-6585","authenticated-orcid":true,"given":"Michael","family":"Overduin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9401-140X","authenticated-orcid":true,"given":"Gustavo","family":"Basurto-Islas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"266","published-online":{"date-parts":[[2025,7,17]]},"reference":[{"key":"prgbadea02bib1","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1586\/ern.10.27","article-title":"Causes versus effects: the increasing complexities of Alzheimer\u2019s disease pathogenesis","volume":"10","author":"Mondragon-Rodriguez","year":"2010","journal-title":"Expert Rev. Neurother"},{"key":"prgbadea02bib2","doi-asserted-by":"publisher","first-page":"15824","DOI":"10.1073\/pnas.0605629103","article-title":"Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer\u2019s Abeta42 peptide","volume":"103","author":"Kim","year":"2006","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"prgbadea02bib3","doi-asserted-by":"publisher","first-page":"3203","DOI":"10.1111\/febs.16738","article-title":"Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1\u201342 aggregates","volume":"290","author":"Zhaliazka","year":"2023","journal-title":"FEBS J."},{"key":"prgbadea02bib4","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpc.2024.107248","article-title":"Thermodynamics of oligomerization and Helix-to-sheet structural transition of amyloid beta-protein on anionic phospholipid vesicles","volume":"310","author":"Ikeda","year":"2024","journal-title":"Biophys. Chem."},{"key":"prgbadea02bib5","doi-asserted-by":"publisher","first-page":"1859","DOI":"10.3390\/ijms22041859","article-title":"Promotion and inhibition of amyloid-beta peptide aggregation: molecular dynamics studies","volume":"22","author":"Itoh","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"prgbadea02bib6","doi-asserted-by":"publisher","first-page":"1776","DOI":"10.3390\/molecules27061776","article-title":"Amyloid cross-seeding: mechanism, implication, and inhibition","volume":"27","author":"Subedi","year":"2022","journal-title":"Molecules"},{"key":"prgbadea02bib7","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1248\/cpb.c15-00742","article-title":"Medicinal chemistry focusing on aggregation of amyloid-\u03b2","volume":"64","author":"Sohma","year":"2016","journal-title":"Chem. Pharm. Bull."},{"key":"prgbadea02bib8","doi-asserted-by":"publisher","DOI":"10.1016\/j.abb.2020.108614","article-title":"Sequence and structure-based peptides as potent amyloid inhibitors: a review","volume":"695","author":"Mitra","year":"2020","journal-title":"Arch. Biochem. Biophys."},{"key":"prgbadea02bib9","doi-asserted-by":"publisher","first-page":"54","DOI":"10.3389\/fnmol.2019.00054","article-title":"Structure-based peptide inhibitor design of amyloid-\u03b2 aggregation","volume":"12","author":"Lu","year":"2019","journal-title":"Front. Mol. Neurosci."},{"key":"prgbadea02bib10","doi-asserted-by":"publisher","first-page":"741","DOI":"10.3233\/JAD-215412","article-title":"Multiadducts of C60 modulate amyloid-\u03b2 fibrillation with dual acetylcholinesterase inhibition and antioxidant properties: in vitro and in silico studies","volume":"87","author":"Mart\u00ednez-Herrera","year":"2022","journal-title":"J. Alzheimers Dis."},{"key":"prgbadea02bib11","doi-asserted-by":"publisher","DOI":"10.1016\/j.arr.2019.100948","article-title":"Do anti-amyloid-beta drugs affect neuropsychiatric status in Alzheimer\u2019s disease patients?","volume":"55","author":"Panza","year":"2019","journal-title":"Ageing Res. Rev."},{"key":"prgbadea02bib12","first-page":"1020","article-title":"Electromagnetic field stimulation therapy for Alzheimer\u2019s disease","volume":"3","author":"Perez","year":"2024","journal-title":"Neurology"},{"key":"prgbadea02bib13","doi-asserted-by":"publisher","DOI":"10.1063\/1.4941108","article-title":"Electromagnetic-field effects on structure and dynamics of amyloidogenic peptides","volume":"144","author":"Todorova","year":"2016","journal-title":"J. Chem. Phys."},{"key":"prgbadea02bib14","doi-asserted-by":"publisher","first-page":"1","DOI":"10.2741\/e781","article-title":"Mechanisms of protein aggregation and inhibition","volume":"9","author":"Siddiqi","year":"2017","journal-title":"Front. Biosci."},{"key":"prgbadea02bib15","doi-asserted-by":"publisher","first-page":"24251","DOI":"10.1073\/pnas.2006684117","article-title":"Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors","volume":"117","author":"Michaels","year":"2020","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"prgbadea02bib16","doi-asserted-by":"publisher","first-page":"57","DOI":"10.3233\/JAD-190367","article-title":"A clinical trial of transcranial electromagnetic treatment in Alzheimer\u2019s disease: cognitive enhancement and associated changes in cerebrospinal fluid, blood, and brain imaging","volume":"71","author":"Arendash","year":"2019","journal-title":"J. Alzheimers Dis."},{"key":"prgbadea02bib17","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1016\/j.neuroscience.2011.04.012","article-title":"Long-term electromagnetic field treatment enhances brain mitochondrial function of both Alzheimer\u2019s transgenic mice and normal mice: a mechanism for electromagnetic field-induced cognitive benefit?","volume":"185","author":"Dragicevic","year":"2011","journal-title":"Neuroscience"},{"key":"prgbadea02bib18","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1002\/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7","article-title":"Why are \u201cnatively unfolded\u201d proteins unstructured under physiologic conditions?","volume":"41","author":"Uversky","year":"2000","journal-title":"Proteins"},{"key":"prgbadea02bib19","doi-asserted-by":"publisher","first-page":"e4643","DOI":"10.1002\/pro.4643","article-title":"Electronegative clusters modulate folding status and RNA binding of unstructured RNA-binding proteins","volume":"32","author":"Zaharias","year":"2023","journal-title":"Protein Sci."},{"key":"prgbadea02bib20","doi-asserted-by":"publisher","first-page":"336","DOI":"10.1002\/prot.1099","article-title":"Prediction of protein interaction sites from sequence profile and residue neighbor list","volume":"44","author":"Zhou","year":"2001","journal-title":"Proteins"},{"key":"prgbadea02bib21","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pcbi.1003192","article-title":"On the importance of polar interactions for complexes containing intrinsically disordered proteins","volume":"9","author":"Wong","year":"2013","journal-title":"PLoS Comput. Biol."},{"key":"prgbadea02bib22","doi-asserted-by":"publisher","first-page":"885","DOI":"10.1016\/S1357-2725(99)00027-8","article-title":"Amyloid beta","volume":"31","author":"Cappai","year":"1999","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"prgbadea02bib23","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1006\/jmbi.1995.0525","article-title":"Self-association of beta-amyloid peptide (1\u201340) in solution and binding to lipid membranes","volume":"252","author":"Terzi","year":"1995","journal-title":"J. Mol. Biol."},{"key":"prgbadea02bib24","doi-asserted-by":"publisher","first-page":"220","DOI":"10.1002\/prot.10468","article-title":"Mechanism for the alpha-helix to beta-hairpin transition","volume":"53","author":"Ding","year":"2003","journal-title":"Proteins"},{"key":"prgbadea02bib25","doi-asserted-by":"publisher","first-page":"16742","DOI":"10.1073\/pnas.262663499","article-title":"A structural model for Alzheimer\u2019s beta -amyloid fibrils based on experimental constraints from solid state NMR","volume":"99","author":"Petkova","year":"2002","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"prgbadea02bib26","doi-asserted-by":"publisher","first-page":"1528","DOI":"10.1002\/pro.2544","article-title":"Physical and structural basis for polymorphism in amyloid fibrils","volume":"23","author":"Tycko","year":"2014","journal-title":"Protein Sci."},{"key":"prgbadea02bib27","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1016\/S0006-3495(95)79940-4","article-title":"Solvent effects on self-assembly of beta-amyloid peptide","volume":"69","author":"Shen","year":"1995","journal-title":"Biophys. J."},{"key":"prgbadea02bib28","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1006\/jsbi.2000.4221","article-title":"Review: history of the amyloid fibril","volume":"130","author":"Sipe","year":"2000","journal-title":"J. Struct. Biol."},{"key":"prgbadea02bib29","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1177\/16.11.673","article-title":"X-ray diffraction studies on amyloid filaments","volume":"16","author":"Eanes","year":"1968","journal-title":"J. Histochem. Cytochem."},{"key":"prgbadea02bib30","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1146\/annurev.biochem.66.1.385","article-title":"Models of amyloid seeding in Alzheimer\u2019s disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins","volume":"66","author":"Harper","year":"1997","journal-title":"Annu. Rev. Biochem."},{"key":"prgbadea02bib31","doi-asserted-by":"publisher","first-page":"2497","DOI":"10.1021\/bi7019194","article-title":"Beta2-microglobulin amyloid fragment organization and morphology and its comparison to Abeta suggests that amyloid aggregation pathways are sequence specific","volume":"47","author":"Zheng","year":"2008","journal-title":"Biochemistry"},{"key":"prgbadea02bib32","doi-asserted-by":"publisher","first-page":"6968","DOI":"10.1021\/bi500674u","article-title":"The importance of being capped: terminal capping of an amyloidogenic peptide affects fibrillation propensity and fibril morphology","volume":"53","author":"Andreasen","year":"2014","journal-title":"Biochemistry"},{"key":"prgbadea02bib33","doi-asserted-by":"publisher","first-page":"1125","DOI":"10.1073\/pnas.93.3.1125","article-title":"On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants","volume":"93","author":"Lomakin","year":"1996","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"prgbadea02bib34","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1002\/chem.202400277","article-title":"Aggregation mechanisms and molecular structures of amyloid-beta in Alzheimer\u2019s disease","volume":"30","author":"Niu","year":"2024","journal-title":"Chemistry"},{"key":"prgbadea02bib35","doi-asserted-by":"publisher","first-page":"e4639","DOI":"10.1002\/pro.4639","article-title":"Structural polymorphism and cytotoxicity of brain-derived \u03b2-amyloid extracts","volume":"32","author":"Al Adem","year":"2023","journal-title":"Protein Sci."},{"key":"prgbadea02bib36","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1073\/pnas.2023089118","article-title":"Molecular structure of a prevalent amyloid-\u03b2 fibril polymorph from Alzheimer\u2019s disease brain tissue","volume":"118","author":"Ghosh","year":"2021","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"prgbadea02bib37","doi-asserted-by":"publisher","first-page":"498","DOI":"10.1021\/bi051952q","article-title":"Experimental constraints on quaternary structure in Alzheimer\u2019s beta-amyloid fibrils","volume":"45","author":"Petkova","year":"2006","journal-title":"Biochemistry"},{"key":"prgbadea02bib38","doi-asserted-by":"publisher","first-page":"7133","DOI":"10.1021\/bi00483a001","article-title":"Dominant forces in protein folding","volume":"29","author":"Dill","year":"1990","journal-title":"Biochemistry"},{"key":"prgbadea02bib39","doi-asserted-by":"publisher","first-page":"1677","DOI":"10.1021\/acschembio.9b00339","article-title":"Secondary forces in protein folding","volume":"14","author":"Newberry","year":"2019","journal-title":"ACS Chem. Biol."},{"key":"prgbadea02bib40","doi-asserted-by":"publisher","first-page":"460","DOI":"10.1016\/0022-2836(92)90835-8","article-title":"Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer\u2019s disease beta A4 peptides","volume":"228","author":"Hilbich","year":"1992","journal-title":"J. Mol. Biol."},{"key":"prgbadea02bib41","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1016\/j.jmb.2007.05.078","article-title":"Energetics of protein folding","volume":"371","author":"Baldwin","year":"2007","journal-title":"J. Mol. Biol."},{"key":"prgbadea02bib42","doi-asserted-by":"publisher","first-page":"604","DOI":"10.1002\/1439-7633(20020703)3:7<604::AID-CBIC604>3.0.CO;2-X","article-title":"Close-range electrostatic interactions in proteins","volume":"3","author":"Kumar","year":"2002","journal-title":"Chembiochem"},{"key":"prgbadea02bib43","doi-asserted-by":"publisher","first-page":"601","DOI":"10.2174\/1389203023380431","article-title":"Electrostatics in protein binding and function","volume":"3","author":"Sinha","year":"2002","journal-title":"Curr. Protein Pept Sci."},{"key":"prgbadea02bib44","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.07454","article-title":"Contacts-based prediction of binding affinity in protein-protein complexes","volume":"4","author":"Vangone","year":"2015","journal-title":"eLife"},{"key":"prgbadea02bib45","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-023-37130-z","article-title":"Electrostatic complementarity at the interface drives transient protein-protein interactions","volume":"13","author":"Grassmann","year":"2023","journal-title":"Sci. Rep."},{"key":"prgbadea02bib46","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1126\/science.1105850","article-title":"Self-propagating, molecular-level polymorphism in Alzheimer\u2019s beta-amyloid fibrils","volume":"307","author":"Petkova","year":"2005","journal-title":"Science"},{"key":"prgbadea02bib47","doi-asserted-by":"publisher","first-page":"571","DOI":"10.3390\/ijms19020571","article-title":"Conformational dynamics and stability of U-shaped and S-shaped amyloid \u03b2 assemblies","volume":"19","author":"Grasso","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"prgbadea02bib48","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1016\/S0969-2126(00)00183-0","article-title":"Mutational analysis of designed peptides that undergo structural transition from alpha helix to beta sheet and amyloid fibril formation","volume":"8","author":"Takahashi","year":"2000","journal-title":"Structure"},{"key":"prgbadea02bib49","doi-asserted-by":"publisher","first-page":"1427","DOI":"10.1021\/acs.jpclett.2c03729","article-title":"Familial Alzheimer\u2019s disease-related mutations differentially alter stability of amyloid-beta aggregates","volume":"14","author":"Rezaei-Ghaleh","year":"2023","journal-title":"J. Phys. Chem. Lett."},{"key":"prgbadea02bib50","doi-asserted-by":"publisher","first-page":"E5849","DOI":"10.1073\/pnas.1803539115","article-title":"On the role of sidechain size and charge in the aggregation of A\u03b242 with familial mutations","volume":"115","author":"Yang","year":"2018","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"prgbadea02bib51","doi-asserted-by":"publisher","first-page":"12243","DOI":"10.1073\/pnas.91.25.12243","article-title":"Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red","volume":"91","author":"Lorenzo","year":"1994","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"prgbadea02bib52","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1016\/0304-3940(95)11939-T","article-title":"Sulfonated dyes attenuate the toxic effects of beta-amyloid in a structure-specific fashion","volume":"197","author":"Pollack","year":"1995","journal-title":"Neurosci Lett."},{"key":"prgbadea02bib53","doi-asserted-by":"publisher","first-page":"4086","DOI":"10.1074\/jbc.271.8.4086","article-title":"Selective inhibition of Abeta fibril formation","volume":"271","author":"Wood","year":"1996","journal-title":"J. Biol. Chem."},{"key":"prgbadea02bib54","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1016\/0014-5793(94)80467-2","article-title":"beta-Cyclodextrin interacts with the Alzheimer amyloid beta-A4 peptide","volume":"341","author":"Camilleri","year":"1994","journal-title":"FEBS Lett."},{"key":"prgbadea02bib55","doi-asserted-by":"publisher","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."},{"key":"prgbadea02bib56","doi-asserted-by":"publisher","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."},{"key":"prgbadea02bib57","doi-asserted-by":"publisher","first-page":"191","DOI":"10.3233\/JAD-2010-1228","article-title":"Electromagnetic field treatment protects against and reverses cognitive impairment in Alzheimer\u2019s disease mice","volume":"19","author":"Arendash","year":"2010","journal-title":"J. Alzheimers Dis."},{"key":"prgbadea02bib58","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-020-74431-z","article-title":"Individual head models for estimating the TMS-induced electric field in rat brain","volume":"10","author":"Koponen","year":"2020","journal-title":"Sci. Rep."},{"key":"prgbadea02bib59","doi-asserted-by":"publisher","first-page":"1257","DOI":"10.1152\/jn.00716.2011","article-title":"Parameterization of transcranial magnetic stimulation","volume":"107","author":"Rubens","year":"2012","journal-title":"J. Neurophysiol."},{"key":"prgbadea02bib60","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1002\/cphc.202200646","article-title":"Capturing the polarization response of solvated proteins under constant electric fields in molecular dynamics simulations","volume":"24","author":"Chakraborty","year":"2023","journal-title":"Chemphyschem"},{"key":"prgbadea02bib61","doi-asserted-by":"publisher","first-page":"3516","DOI":"10.1021\/ct1001335","article-title":"Electric field effects on short fibrils of A\u03b2 amyloid peptides","volume":"6","author":"Lugli","year":"2010","journal-title":"J. Chem. Theory Comput."},{"key":"prgbadea02bib62","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1021\/jp807896g","article-title":"Effects of electric field stress on a \u03b2-amyloid peptide","volume":"113","author":"Toschi","year":"2009","journal-title":"J. Phys. Chem. A"},{"key":"prgbadea02bib63","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmgm.2020.107535","article-title":"Elucidating the effect of static electric field on amyloid beta 1\u201342 supramolecular assembly","volume":"96","author":"Muscat","year":"2020","journal-title":"J. Mol. Graph. Model."},{"key":"prgbadea02bib64","doi-asserted-by":"publisher","DOI":"10.1063\/1.5018459","article-title":"Influence of electric field on the amyloid-beta(29\u201342) peptides embedded in a membrane bilayer","volume":"148","author":"Lu","year":"2018","journal-title":"J. Chem. Phys."},{"key":"prgbadea02bib65","doi-asserted-by":"publisher","first-page":"123","DOI":"10.3390\/polym14010123","article-title":"Effects of an electric field on the conformational transition of the protein: pulsed and oscillating electric fields with different frequencies","volume":"14","author":"Zhang","year":"2021","journal-title":"Polymers"},{"key":"prgbadea02bib66","doi-asserted-by":"publisher","first-page":"282","DOI":"10.3390\/polym11020282","article-title":"Effects of an electric field on the conformational transition of the protein: a molecular dynamics simulation study","volume":"11","author":"Jiang","year":"2019","journal-title":"Polymers"},{"key":"prgbadea02bib67","doi-asserted-by":"publisher","DOI":"10.1063\/1.5126367","article-title":"Electromagnetic field modulates aggregation propensity of amyloid peptides","volume":"152","author":"Todorova","year":"2020","journal-title":"J. Chem. Phys."},{"key":"prgbadea02bib68","doi-asserted-by":"publisher","first-page":"6312","DOI":"10.3390\/ijms24076312","article-title":"Effect of electric field on \u03b1-synuclein fibrils: revealed by molecular dynamics simulations","volume":"24","author":"Razzokov","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"prgbadea02bib69","doi-asserted-by":"publisher","first-page":"2431","DOI":"10.1016\/j.clinph.2004.05.031","article-title":"Selection of stimulus parameters for deep brain stimulation","volume":"115","author":"Kuncel","year":"2004","journal-title":"Clin. Neurophysiol."},{"key":"prgbadea02bib70","doi-asserted-by":"publisher","first-page":"22641","DOI":"10.1021\/jp052742q","article-title":"Electric field effects on insulin chain-B conformation","volume":"109","author":"Budi","year":"2005","journal-title":"J. Phys. Chem. B"},{"key":"prgbadea02bib71","doi-asserted-by":"publisher","first-page":"5748","DOI":"10.1021\/jp067248g","article-title":"Effect of frequency on insulin response to electric field stress","volume":"111","author":"Budi","year":"2007","journal-title":"J. Phys. Chem. B"},{"key":"prgbadea02bib72","doi-asserted-by":"publisher","first-page":"8942","DOI":"10.1021\/jp501051r","article-title":"Effect of strong electric field on the conformational integrity of insulin","volume":"118","author":"Wang","year":"2014","journal-title":"J. Phys. Chem. A"},{"key":"prgbadea02bib73","doi-asserted-by":"publisher","first-page":"4128","DOI":"10.1021\/acschemneuro.3c00485","article-title":"Effect of terahertz waves on the structure of the Abeta42 monomer, dimer, and protofibril: insights from molecular dynamics simulations","volume":"14","author":"Chen","year":"2023","journal-title":"ACS Chem. Neurosci."},{"key":"prgbadea02bib74","first-page":"1","article-title":"Devices, facilities, and shielding for biological experiments with static and extremely low frequency magnetic fields","volume":"9","author":"Makinistian","year":"2024","journal-title":"IEEE J. Electromagn. RF Microw. Med. Biol."},{"key":"prgbadea02bib75","doi-asserted-by":"publisher","first-page":"2250","DOI":"10.1021\/acschemneuro.8b00490","article-title":"Electric field disruption of amyloid aggregation: potential noninvasive therapy for Alzheimer\u2019s disease","volume":"10","author":"Saikia","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"prgbadea02bib76","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/j.neulet.2007.02.057","article-title":"Fifty Hertz electromagnetic field exposure stimulates secretion of beta-amyloid peptide in cultured human neuroglioma","volume":"418","author":"Del Giudice","year":"2007","journal-title":"Neurosci Lett."},{"key":"prgbadea02bib77","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/S1567-5394(02)00004-X","article-title":"Effects of 60 Hz electromagnetic field exposure on APP695 transcription levels in differentiating human neuroblastoma cells","volume":"57","author":"Rao","year":"2002","journal-title":"Bioelectrochemistry"},{"key":"prgbadea02bib78","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1080\/15368378.2020.1830288","article-title":"Low frequency vortex magnetic field reduces amyloid \u03b2 aggregation, increase cell viability and protect from amyloid \u03b2 toxicity","volume":"40","author":"Maldonado-Moreles","year":"2021","journal-title":"Electromagn. Biol. Med."},{"key":"prgbadea02bib79","doi-asserted-by":"publisher","DOI":"10.31349\/RevMexFis.70.030901","article-title":"Vortex magnetic induction: mathematical, geometric and experimental characterization","volume":"70","author":"Ram\u00edrez Galindo","year":"2024","journal-title":"Rev. Mex. Fis."},{"key":"prgbadea02bib80","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1002\/bem.22400","article-title":"An extremely low-frequency vortex magnetic field modifies protein expression, rearranges the cytoskeleton, and induces apoptosis of a human neuroblastoma cell line","volume":"43","author":"Aparicio-Bautista","year":"2022","journal-title":"Bioelectromagnetics"},{"key":"prgbadea02bib81","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/j.bpc.2017.04.004","article-title":"Fibrillar disruption by AC electric field induced oscillation: a case study with human serum albumin","volume":"226","author":"Sen","year":"2017","journal-title":"Biophys. Chem."},{"key":"prgbadea02bib82","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1046\/j.1471-4159.2003.01552.x","article-title":"Cholesterol is necessary both for the toxic effect of Abeta peptides on vascular smooth muscle cells and for Abeta binding to vascular smooth muscle cell membranes","volume":"84","author":"Subasinghe","year":"2003","journal-title":"J. Neurochem."},{"key":"prgbadea02bib83","doi-asserted-by":"publisher","first-page":"14845","DOI":"10.1021\/bi971843e","article-title":"Interaction of Alzheimer beta-amyloid peptide(1\u201340) with lipid membranes","volume":"36","author":"Terzi","year":"1997","journal-title":"Biochemistry"},{"key":"prgbadea02bib84","doi-asserted-by":"publisher","first-page":"4137","DOI":"10.1021\/bi982345o","article-title":"Interactions of amyloid beta-peptide (1\u201340) with ganglioside-containing membranes","volume":"38","author":"Matsuzaki","year":"1999","journal-title":"Biochemistry"},{"key":"prgbadea02bib85","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1016\/j.abb.2007.11.004","article-title":"A comparative molecular dynamics analysis of the amyloid beta-peptide in a lipid bilayer","volume":"470","author":"Lemkul","year":"2008","journal-title":"Arch. Biochem. Biophys."},{"key":"prgbadea02bib86","doi-asserted-by":"publisher","first-page":"458","DOI":"10.1002\/(SICI)1097-4547(19990815)57:4<458::AID-JNR5>3.0.CO;2-4","article-title":"Alzheimer amyloid abeta1-42 channels: effects of solvent, pH, and Congo Red","volume":"57","author":"Hirakura","year":"1999","journal-title":"J. Neurosci. Res."},{"key":"prgbadea02bib87","doi-asserted-by":"publisher","first-page":"934","DOI":"10.1016\/S0006-3495(00)76348-X","article-title":"Displacement currents associated with the insertion of Alzheimer disease amyloid beta-peptide into planar bilayer membranes","volume":"79","author":"Vargas","year":"2000","journal-title":"Biophys. J."},{"key":"prgbadea02bib88","doi-asserted-by":"publisher","first-page":"178","DOI":"10.1016\/j.arcmed.2013.03.005","article-title":"Electromagnetic pulse exposure induces overexpression of beta amyloid protein in rats","volume":"44","author":"Jiang","year":"2013","journal-title":"Arch. Med. Res."},{"key":"prgbadea02bib89","doi-asserted-by":"publisher","first-page":"70","DOI":"10.4103\/2152-7806.185006","article-title":"The effects of 30 mT electromagnetic fields on hippocampus cells of rats","volume":"7","author":"Teimori","year":"2016","journal-title":"Surg. Neurol. Int."},{"key":"prgbadea02bib90","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1016\/j.brainres.2015.01.019","article-title":"Exposure to 900 MHz electromagnetic fields activates the mkp-1\/ERK pathway and causes blood-brain barrier damage and cognitive impairment in rats","volume":"1601","author":"Tang","year":"2015","journal-title":"Brain Res."},{"key":"prgbadea02bib91","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0035751","article-title":"Electromagnetic treatment to old Alzheimer\u2019s mice reverses beta-amyloid deposition, modifies cerebral blood flow, and provides selected cognitive benefit","volume":"7","author":"Arendash","year":"2012","journal-title":"PLoS One"},{"key":"prgbadea02bib92","doi-asserted-by":"publisher","first-page":"481","DOI":"10.2174\/156720501205150526114448","article-title":"1950 MHz electromagnetic fields ameliorate abeta pathology in Alzheimer\u2019s disease mice","volume":"12","author":"Jeong","year":"2015","journal-title":"Curr. Alzheimer Res."},{"key":"prgbadea02bib93","doi-asserted-by":"publisher","first-page":"28","DOI":"10.3109\/09553002.2014.954058","article-title":"Short-term effects of extremely low frequency electromagnetic fields exposure on Alzheimer\u2019s disease in rats","volume":"91","author":"Zhang","year":"2015","journal-title":"Int. J. Radiat. Biol."},{"key":"prgbadea02bib94","doi-asserted-by":"publisher","first-page":"391","DOI":"10.1002\/bem.21992","article-title":"1950 MHz radiofrequency electromagnetic fields do not aggravate memory deficits in 5xFAD mice","volume":"37","author":"Son","year":"2016","journal-title":"Bioelectromagnetics"},{"key":"prgbadea02bib95","doi-asserted-by":"publisher","first-page":"8585","DOI":"10.1038\/srep08585","article-title":"Low-frequency magnetic fields do not aggravate disease in mouse models of Alzheimer\u2019s disease and amyotrophic lateral sclerosis","volume":"5","author":"Liebl","year":"2015","journal-title":"Sci. Rep."},{"key":"prgbadea02bib96","doi-asserted-by":"publisher","DOI":"10.3390\/ijms242216456","article-title":"Magnetic stimulation as a therapeutic approach for brain modulation and repair: underlying molecular and cellular mechanisms","volume":"24","author":"Dufor","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"prgbadea02bib97","doi-asserted-by":"publisher","first-page":"4455","DOI":"10.3390\/en15124455","article-title":"Biological and medical disturbances due to exposure to fields emitted by electromagnetic energy devices\u2014a review","volume":"15","author":"Razek","year":"2022","journal-title":"Energies"},{"key":"prgbadea02bib98","doi-asserted-by":"publisher","first-page":"4474","DOI":"10.1002\/adma.200700590","article-title":"Alignment of aromatic peptide tubes in strong magnetic fields","volume":"19","author":"Hill","year":"2007","journal-title":"Adv. Mater."},{"key":"prgbadea02bib99","author":"Jackson","year":"2021"},{"key":"prgbadea02bib100","doi-asserted-by":"publisher","first-page":"S3","DOI":"10.33588\/rn.46S01.2008081","article-title":"Estimulaci\u00f3n magn\u00e9tica transcraneal: fundamentos y potencial de la modulaci\u00f3n de redes neurales espec\u00edficas","volume":"46","author":"Pascual-Leone","year":"2008","journal-title":"Rev. Neurol."},{"key":"prgbadea02bib101","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1146\/annurev.bb.15.060186.001115","article-title":"Electrostatic interactions in membranes and proteins","volume":"15","author":"Honig","year":"1986","journal-title":"Ann. Rev. Biophys. Biophys. Chem."},{"key":"prgbadea02bib102","doi-asserted-by":"publisher","first-page":"16198","DOI":"10.1039\/C9CP01542F","article-title":"Electric field influence on the helical structure of peptides: insights from DFT\/PCM computations","volume":"21","author":"Ilieva","year":"2019","journal-title":"Phys. Chem. Chem. Phys."},{"key":"prgbadea02bib103","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1186\/s12929-022-00825-y","article-title":"Multidimensional insights into the repeated electromagnetic field stimulation and biosystems interaction in aging and age-related diseases","volume":"29","author":"Perez","year":"2022","journal-title":"J. Biomed. Sci."},{"key":"prgbadea02bib104","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1016\/j.clinph.2020.10.003","article-title":"Safety and recommendations for TMS use in healthy subjects and patient populations, with updates on training, ethical and regulatory issues: expert guidelines","volume":"132","author":"Rossi","year":"2021","journal-title":"Clin. Neurophysiol."}],"container-title":["Progress in Biomedical Engineering"],"original-title":[],"link":[{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02","content-type":"text\/html","content-version":"am","intended-application":"text-mining"},{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02\/pdf","content-type":"application\/pdf","content-version":"am","intended-application":"text-mining"},{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02\/pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02\/pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02\/pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02\/pdf","content-type":"application\/pdf","content-version":"am","intended-application":"similarity-checking"},{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02\/pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,7,17]],"date-time":"2025-07-17T09:45:07Z","timestamp":1752745507000},"score":1,"resource":{"primary":{"URL":"https:\/\/iopscience.iop.org\/article\/10.1088\/2516-1091\/adea02"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,7,1]]},"references-count":104,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2025,7,17]]},"published-print":{"date-parts":[[2025,7,1]]}},"URL":"https:\/\/doi.org\/10.1088\/2516-1091\/adea02","relation":{},"ISSN":["2516-1091"],"issn-type":[{"value":"2516-1091","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,7,1]]},"assertion":[{"value":"Molecular mechanisms associated with the interaction of external electromagnetic fields in protein dynamics and aggregation: a focus on amyloid-\u03b2 peptide","name":"article_title","label":"Article Title"},{"value":"Progress in Biomedical Engineering","name":"journal_title","label":"Journal Title"},{"value":"paper","name":"article_type","label":"Article Type"},{"value":"\u00a9 2025 The Author(s). Published by IOP Publishing Ltd","name":"copyright_information","label":"Copyright Information"},{"value":"2024-11-06","name":"date_received","label":"Date Received","group":{"name":"publication_dates","label":"Publication dates"}},{"value":"2025-06-30","name":"date_accepted","label":"Date Accepted","group":{"name":"publication_dates","label":"Publication dates"}},{"value":"2025-07-17","name":"date_epub","label":"Online publication date","group":{"name":"publication_dates","label":"Publication dates"}}]}}