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Mutations in A\u03b2 are associated with early onset familial AD, and the Arctic mutant E22G (A\u03b2arc) is an extremely aggregation-prone variant. Here, we show that BRICHOS, a natural anti-amyloid chaperone domain, from Bri2 efficiently inhibits aggregation of A\u03b2arc by mainly interfering with secondary nucleation. This is qualitatively different from the microscopic inhibition mechanism for the wild-type A\u03b2, against which Bri2 BRICHOS has a major effect on both secondary nucleation and fibril end elongation. The monomeric A\u03b242arc peptide aggregates into amyloid fibrils significantly faster than wild-type A\u03b2 (A\u03b242wt), as monitored by thioflavin T (ThT) binding, but the final ThT intensity was strikingly lower for A\u03b242arc compared to A\u03b242wt fibrils. The A\u03b242arc peptide formed large aggregates, single-filament fibrils, and multiple-filament fibrils without obvious twists, while A\u03b242wt fibrils displayed a polymorphic pattern with typical twisted fibril architecture. Recombinant human Bri2 BRICHOS binds to the A\u03b242arc fibril surface and interferes with the macroscopic fibril arrangement by promoting single-filament fibril formation. This study provides mechanistic insights on how BRICHOS efficiently affects the aggressive A\u03b242arc aggregation, resulting in both delayed fibril formation kinetics and altered fibril structure.<\/jats:p>","DOI":"10.1021\/acschembio.2c00344","type":"journal-article","created":{"date-parts":[[2022,7,25]],"date-time":"2022-07-25T10:24:05Z","timestamp":1658744645000},"page":"2201-2211","source":"Crossref","is-referenced-by-count":23,"title":["Amyloid Fibril\nFormation of Arctic Amyloid\u2011\u03b2\n1\u201342 Peptide is Efficiently Inhibited by the BRICHOS Domain"],"prefix":"10.1021","volume":"17","author":[{"given":"Xueying","family":"Zhong","sequence":"first","affiliation":[{"name":"KTH Royal Institute of Technology , , ,","place":["Huddinge, Sweden, 141 52"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rakesh","family":"Kumar","sequence":"additional","affiliation":[{"name":"Karolinska Institutet , , ,","place":["Huddinge, Sweden, 141 52"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Wang","sequence":"additional","affiliation":[{"name":"Karolinska Institutet , , ,","place":["Huddinge, Sweden, 141 52"]},{"name":"Northeast Forestry University , , ,","place":["Harbin, People\u2019s Republic of China, 150040"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2097-7658","authenticated-orcid":true,"given":"Henrik","family":"Biverst\u00e5l","sequence":"additional","affiliation":[{"name":"Karolinska Institutet , , ,","place":["Huddinge, Sweden, 141 52"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caroline","family":"Ingeborg Jegerscho\u0308ld","sequence":"additional","affiliation":[{"name":"KTH Royal Institute of Technology , , ,","place":["Huddinge, Sweden, 141 52"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip","family":"J B Koeck","sequence":"additional","affiliation":[{"name":"KTH Royal Institute of Technology , , ,","place":["Huddinge, Sweden, 141 52"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8719-4703","authenticated-orcid":true,"given":"Jan","family":"Johansson","sequence":"additional","affiliation":[{"name":"Karolinska Institutet , , ,","place":["Huddinge, Sweden, 141 52"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8079-3017","authenticated-orcid":true,"given":"Axel","family":"Abelein","sequence":"additional","affiliation":[{"name":"Karolinska Institutet , , ,","place":["Huddinge, Sweden, 141 52"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5543-5963","authenticated-orcid":true,"given":"Gefei","family":"Chen","sequence":"additional","affiliation":[{"name":"Karolinska Institutet , , ,","place":["Huddinge, Sweden, 141 52"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2022,7,25]]},"reference":[{"key":"2026081413081392300_cit1","doi-asserted-by":"publisher","first-page":"209","DOI":"10.1080\/13506129.2016.1257986","article-title":"Amyloid fibril proteins and amyloidosis:\nchemical identification and clinical classification International\nSociety of Amyloidosis 2016 Nomenclature Guidelines","volume":"23","author":"Sipe","year":"2016","journal-title":"Amyloid"},{"key":"2026081413081392300_cit2","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1111\/joim.12500","article-title":"The formation, function\nand regulation\nof amyloids: insights from structural biology","volume":"280","author":"Landreh","year":"2016","journal-title":"J. Intern. Med."},{"key":"2026081413081392300_cit3","doi-asserted-by":"publisher","first-page":"1125","DOI":"10.1038\/s41594-020-0505-6","article-title":"Kinetic fingerprints\ndifferentiate the mechanisms of action of anti-A\u03b2 antibodies","volume":"27","author":"Linse","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026081413081392300_cit4","doi-asserted-by":"publisher","first-page":"595","DOI":"10.15252\/emmm.201606210","article-title":"The amyloid hypothesis of Alzheimer\u2019s disease at 25 years","volume":"8","author":"Selkoe","year":"2016","journal-title":"EMBO Mol. Med."},{"key":"2026081413081392300_cit5","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1186\/alzrt107","article-title":"Molecular consequences\nof amyloid precursor protein and presenilin\nmutations causing autosomal-dominant Alzheimer\u2019s disease","volume":"4","author":"Weggen","year":"2012","journal-title":"Alzheimer\u2019s Res. Ther."},{"key":"2026081413081392300_cit6","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1016\/j.cell.2017.07.004","article-title":"Alzheimer\u2019s-Causing\nMutations Shift\nA\u03b2 Length by Destabilizing \u03b3-Secretase-A\u03b2n Interactions","volume":"170","author":"Szaruga","year":"2017","journal-title":"Cell"},{"key":"2026081413081392300_cit7","doi-asserted-by":"publisher","first-page":"E5849","DOI":"10.1073\/pnas.1803539115","article-title":"On the role of sidechain\nsize and charge in the aggregation\nof A \u03b2 42 with familial mutations","volume":"115","author":"Yang","year":"2018","journal-title":"Proc.\nNatl. Acad. Sci. U.S.A."},{"key":"2026081413081392300_cit8","doi-asserted-by":"publisher","first-page":"887","DOI":"10.1038\/nn0901-887","article-title":"The \u201cArctic\u201d APP mutation (E693G)\ncauses Alzheimer\u2019s disease by enhanced A\u03b2 protofibril\nformation","volume":"4","author":"Nilsberth","year":"2001","journal-title":"Nat. Neurosci."},{"key":"2026081413081392300_cit9","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1007\/978-1-4939-7816-8_12","article-title":"Kinetic Analysis\nof Amyloid Formation","volume":"1779","author":"Meisl","year":"2018","journal-title":"Methods Mol. Biol."},{"key":"2026081413081392300_cit10","doi-asserted-by":"publisher","first-page":"9758","DOI":"10.1073\/pnas.1218402110","article-title":"Proliferation of\namyloid-\u03b242\naggregates occurs through a secondary nucleation mechanism","volume":"110","author":"Cohen","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026081413081392300_cit11","doi-asserted-by":"publisher","first-page":"4760","DOI":"10.1038\/s41467-019-12683-8","article-title":"Cryo-EM structure and polymorphism\nof A\u03b2 amyloid fibrils purified from Alzheimer\u2019s brain\ntissue","volume":"10","author":"Kollmer","year":"2019","journal-title":"Nat. Commun."},{"key":"2026081413081392300_cit12","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1126\/science.abm7285","article-title":"Cryo-EM structures of amyloid-\u03b2 42 filaments\nfrom human brains","volume":"375","author":"Yang","year":"2022","journal-title":"Science"},{"key":"2026081413081392300_cit13","doi-asserted-by":"publisher","first-page":"7509","DOI":"10.1021\/jacs.5b03997","article-title":"High Resolution Structural Characterization of A\u03b242\nAmyloid Fibrils by Magic Angle Spinning NMR","volume":"137","author":"Colvin","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"2026081413081392300_cit14","doi-asserted-by":"publisher","first-page":"E4976","DOI":"10.1073\/pnas.1600749113","article-title":"Atomic-resolution\nstructure of a disease-relevant A\u03b2\u00ad(1-42) amyloid fibril","volume":"113","author":"Wa\u0308lti","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026081413081392300_cit15","doi-asserted-by":"publisher","first-page":"116","DOI":"10.1126\/science.aao2825","article-title":"Fibril structure of\namyloid-\u03b2\u00ad(1-42) by cryo-electron microscopy","volume":"358","author":"Gremer","year":"2017","journal-title":"Science"},{"key":"2026081413081392300_cit16","doi-asserted-by":"publisher","first-page":"aac4354","DOI":"10.1126\/science.aac4354","article-title":"In vivo aspects of protein folding\nand quality control","volume":"353","author":"Balchin","year":"2016","journal-title":"Science"},{"key":"2026081413081392300_cit17","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1016\/j.tips.2013.12.005","article-title":"Chemical kinetics\nfor drug discovery to combat protein aggregation diseases","volume":"35","author":"Arosio","year":"2014","journal-title":"Trends Pharmacol. Sci."},{"key":"2026081413081392300_cit18","doi-asserted-by":"publisher","first-page":"E2752","DOI":"10.1073\/pnas.1715951115","article-title":"BRICHOS domain of Bri2 inhibits islet\namyloid polypeptide (IAPP) fibril formation and toxicity in human\nbeta cells","volume":"115","author":"Oskarsson","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026081413081392300_cit19","doi-asserted-by":"publisher","first-page":"31608","DOI":"10.1074\/jbc.M112.393157","article-title":"BRICHOS Domains Efficiently Delay Fibrillation of Amyloid \u03b2-Peptide","volume":"287","author":"Willander","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2026081413081392300_cit20","doi-asserted-by":"publisher","first-page":"3778","DOI":"10.1021\/bi900135c","article-title":"Anti-Amyloid\nActivity of the C-Terminal Domain of proSP-C against Amyloid \u03b2-Peptide\nand Medin","volume":"48","author":"Nerelius","year":"2009","journal-title":"Biochemistry"},{"key":"2026081413081392300_cit21","doi-asserted-by":"publisher","first-page":"2081","DOI":"10.1038\/s41467-017-02056-4","article-title":"Bri2 BRICHOS client specificity and chaperone\nactivity are governed by assembly state","volume":"8","author":"Chen","year":"2017","journal-title":"Nat.\nCommun."},{"key":"2026081413081392300_cit22","doi-asserted-by":"publisher","first-page":"3683","DOI":"10.1042\/BCJ20160277","article-title":"Dementia-related Bri2\nBRICHOS is a versatile molecular chaperone that efficiently inhibits\nA\u03b242 toxicity in Drosophila","volume":"473","author":"Poska","year":"2016","journal-title":"Biochem.\nJ."},{"key":"2026081413081392300_cit23","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1038\/s42003-020-0757-z","article-title":"Augmentation of Bri2 molecular chaperone\nactivity against amyloid-\u03b2 reduces neurotoxicity in mouse hippocampus\nin vitro","volume":"3","author":"Chen","year":"2020","journal-title":"Commun. Biol."},{"key":"2026081413081392300_cit24","doi-asserted-by":"publisher","first-page":"105992","DOI":"10.1016\/j.pep.2021.105992","article-title":"Optimizing purification\nof the peripheral membrane protein FAM92A1\nfused to a modified spidroin tag","volume":"189","author":"Wang","year":"2022","journal-title":"Protein Expression\nPurif."},{"key":"2026081413081392300_cit25","doi-asserted-by":"publisher","first-page":"105991","DOI":"10.1016\/j.pep.2021.105991","article-title":"A comparison between\nMBP- and NT* as N-terminal fusion partner for recombinant protein\nproduction in E. coli","volume":"189","author":"Raran-Kurussi","year":"2022","journal-title":"Protein Expression Purif."},{"key":"2026081413081392300_cit26","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1016\/j.jbiotec.2020.11.005","article-title":"NT*-HRV3CP: An optimized construct\nof human rhinovirus\n14 3C protease for high-yield expression and fast affinity-tag cleavage","volume":"325","author":"Abdelkader","year":"2021","journal-title":"J. Biotechnol."},{"key":"2026081413081392300_cit27","doi-asserted-by":"publisher","first-page":"2823","DOI":"10.1111\/febs.15169","article-title":"High intracellular\nstability\nof the spidroin N-terminal domain in spite of abundant amyloidogenic\nsegments revealed by in-cell hydrogen\/deuterium exchange mass spectrometry","volume":"287","author":"Kaldma\u0308e","year":"2020","journal-title":"FEBS J."},{"key":"2026081413081392300_cit28","doi-asserted-by":"publisher","first-page":"1873","DOI":"10.1111\/febs.14451","article-title":"A spidroin-derived\nsolubility tag enables controlled aggregation of a designed amyloid\nprotein","volume":"285","author":"Sarr","year":"2018","journal-title":"FEBS J."},{"key":"2026081413081392300_cit29","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1016\/j.imbio.2016.10.015","article-title":"Novel expression of\na functional trimeric fragment of human SP-A with efficacy in neutralisation\nof RSV","volume":"222","author":"Watson","year":"2017","journal-title":"Immunobiology"},{"key":"2026081413081392300_cit30","doi-asserted-by":"publisher","first-page":"15504","DOI":"10.1038\/ncomms15504","article-title":"Efficient protein production inspired\nby how spiders make silk","volume":"8","author":"Kronqvist","year":"2017","journal-title":"Nat. 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Biol."},{"key":"2026081413081392300_cit41","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1038\/nsmb.2971","article-title":"A molecular chaperone\nbreaks the catalytic cycle that generates toxic A\u03b2 oligomers","volume":"22","author":"Cohen","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026081413081392300_cit42","doi-asserted-by":"publisher","first-page":"4857","DOI":"10.1016\/j.cell.2021.08.013","article-title":"The expanding\namyloid family: Structure, stability, function, and pathogenesis","volume":"184","author":"Sawaya","year":"2021","journal-title":"Cell"},{"key":"2026081413081392300_cit43","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1038\/s41583-021-00533-w","article-title":"The probabilistic model of Alzheimer disease:\nthe amyloid hypothesis revised","volume":"23","author":"Frisoni","year":"2022","journal-title":"Nat. Rev. Neurosci."},{"key":"2026081413081392300_cit44","doi-asserted-by":"publisher","first-page":"19813","DOI":"10.1073\/pnas.0905007106","article-title":"Comparison\nof Alzheimer A\u03b2\u00ad(1-40) and A\u03b2\u00ad(1-42)\namyloid fibrils reveals similar protofilament structures","volume":"106","author":"Schmidt","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026081413081392300_cit45","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1016\/j.jsb.2012.06.010","article-title":"Aggregation\nand fibril morphology of the Arctic mutation of Alzheimer\u2019s\nA\u03b2 peptide by CD, TEM, STEM and in situ AFM","volume":"180","author":"Norlin","year":"2012","journal-title":"J. Struct. Biol."},{"key":"2026081413081392300_cit46","doi-asserted-by":"publisher","first-page":"418","DOI":"10.1016\/j.bbrc.2015.01.132","article-title":"Steady-state\nand time-resolved Thioflavin-T fluorescence\ncan report on morphological differences in amyloid fibrils formed\nby A\u03b2\u00ad(1-40) and A\u03b2\u00ad(1-42)","volume":"458","author":"Lindberg","year":"2015","journal-title":"Biochem.\nBiophys. Res. Commun."},{"key":"2026081413081392300_cit47","doi-asserted-by":"publisher","first-page":"2843","DOI":"10.1021\/acschemneuro.9b00068","article-title":"Why A\u03b242\nIs Much More Toxic than A\u03b240","volume":"10","author":"Phillips","year":"2019","journal-title":"ACS Chem.\nNeurosci."},{"key":"2026081413081392300_cit48","doi-asserted-by":"publisher","first-page":"31066","DOI":"10.1074\/jbc.M114.595124","article-title":"Interaction\nof the Molecular Chaperone DNAJB6 with\nGrowing Amyloid-beta 42 (A\u03b242) Aggregates Leads to Sub-stoichiometric\nInhibition of Amyloid Formation","volume":"289","author":"Ma\u030ansson","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2026081413081392300_cit49","doi-asserted-by":"publisher","first-page":"1681","DOI":"10.1016\/j.bpj.2011.07.056","article-title":"Binding of the Molecular Chaperone\n\u03b1B-Crystallin\nto A\u03b2 Amyloid Fibrils Inhibits Fibril Elongation","volume":"101","author":"Shammas","year":"2011","journal-title":"Biophys. 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