Characterization of Uranyl (UO2 2+) Ion Binding to Amyloid Beta (Aβ) Peptides: Effects on Aβ Structure and Aggregation

Uranium (U) is naturally present in ambient air, water, and soil, and depleted uranium (DU) is released into the environment via industrial and military activities. While the radiological damage from U is rather well understood, less is known about the chemical damage mechanisms, which dominate in D...

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Published inACS chemical neuroscience Vol. 14; no. 15; pp. 2618 - 2633
Main Authors Berntsson, Elina, Vosough, Faraz, Noormägi, Andra, Padari, Kärt, Asplund, Fanny, Gielnik, Maciej, Paul, Suman, Jarvet, Jüri, Tõugu, Vello, Roos, Per M., Kozak, Maciej, Gräslund, Astrid, Barth, Andreas, Pooga, Margus, Palumaa, Peep, Wärmländer, Sebastian K. T. S.
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 02.08.2023
Subjects
Alzheimer Disease - metabolism
Alzheimer's disease
Amyloid
amyloid aggregation
Amyloid beta-Peptides - metabolism
Animals
heavy metal toxicity
Ions - chemistry
Medicin och hälsovetenskap
metal-protein binding
neurodegeneration
Uranium
neurodegeneration
metal−protein binding
amyloid aggregation
heavy metal toxicity
Alzheimer’s disease
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Abstract Uranium (U) is naturally present in ambient air, water, and soil, and depleted uranium (DU) is released into the environment via industrial and military activities. While the radiological damage from U is rather well understood, less is known about the chemical damage mechanisms, which dominate in DU. Heavy metal exposure is associated with numerous health conditions, including Alzheimer’s disease (AD), the most prevalent age-related cause of dementia. The pathological hallmark of AD is the deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils in the brain. However, the toxic species in AD are likely oligomeric Aβ aggregates. Exposure to heavy metals such as Cd, Hg, Mn, and Pb is known to increase Aβ production, and these metals bind to Aβ peptides and modulate their aggregation. The possible effects of U in AD pathology have been sparsely studied. Here, we use biophysical techniques to study in vitro interactions between Aβ peptides and uranyl ions, UO2 2+, of DU. We show for the first time that uranyl ions bind to Aβ peptides with affinities in the micromolar range, induce structural changes in Aβ monomers and oligomers, and inhibit Aβ fibrillization. This suggests a possible link between AD and U exposure, which could be further explored by cell, animal, and epidemiological studies. General toxic mechanisms of uranyl ions could be modulation of protein folding, misfolding, and aggregation.
AbstractList Uranium (U) is naturally present in ambient air, water, and soil, and depleted uranium (DU) is released into the environment via industrial and military activities. While the radiological damage from U is rather well understood, less is known about the chemical damage mechanisms, which dominate in DU. Heavy metal exposure is associated with numerous health conditions, including Alzheimer’s disease (AD), the most prevalent age-related cause of dementia. The pathological hallmark of AD is the deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils in the brain. However, the toxic species in AD are likely oligomeric Aβ aggregates. Exposure to heavy metals such as Cd, Hg, Mn, and Pb is known to increase Aβ production, and these metals bind to Aβ peptides and modulate their aggregation. The possible effects of U in AD pathology have been sparsely studied. Here, we use biophysical techniques to study in vitro interactions between Aβ peptides and uranyl ions, UO 2 2+ , of DU. We show for the first time that uranyl ions bind to Aβ peptides with affinities in the micromolar range, induce structural changes in Aβ monomers and oligomers, and inhibit Aβ fibrillization. This suggests a possible link between AD and U exposure, which could be further explored by cell, animal, and epidemiological studies. General toxic mechanisms of uranyl ions could be modulation of protein folding, misfolding, and aggregation.
Uranium (U) is naturally present in ambient air, water, and soil, and depleted uranium (DU) is released into the environment via industrial and military activities. While the radiological damage from U is rather well understood, less is known about the chemical damage mechanisms, which dominate in DU. Heavy metal exposure is associated with numerous health conditions, including Alzheimer’s disease (AD), the most prevalent age-related cause of dementia. The pathological hallmark of AD is the deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils in the brain. However, the toxic species in AD are likely oligomeric Aβ aggregates. Exposure to heavy metals such as Cd, Hg, Mn, and Pb is known to increase Aβ production, and these metals bind to Aβ peptides and modulate their aggregation. The possible effects of U in AD pathology have been sparsely studied. Here, we use biophysical techniques to study in vitro interactions between Aβ peptides and uranyl ions, UO 2 2+ , of DU. We show for the first time that uranyl ions bind to Aβ peptides with affinities in the micromolar range, induce structural changes in Aβ monomers and oligomers, and inhibit Aβ fibrillization. This suggests a possible link between AD and U exposure, which could be further explored by cell, animal, and epidemiological studies. General toxic mechanisms of uranyl ions could be modulation of protein folding, misfolding, and aggregation. 
Uranium (U) is naturally present in ambient air, water, and soil, and depleted uranium (DU) is released into the environment via industrial and military activities. While the radiological damage from U is rather well understood, less is known about the chemical damage mechanisms, which dominate in DU. Heavy metal exposure is associated with numerous health conditions, including Alzheimer’s disease (AD), the most prevalent age-related cause of dementia. The pathological hallmark of AD is the deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils in the brain. However, the toxic species in AD are likely oligomeric Aβ aggregates. Exposure to heavy metals such as Cd, Hg, Mn, and Pb is known to increase Aβ production, and these metals bind to Aβ peptides and modulate their aggregation. The possible effects of U in AD pathology have been sparsely studied. Here, we use biophysical techniques to study in vitro interactions between Aβ peptides and uranyl ions, UO2 2+, of DU. We show for the first time that uranyl ions bind to Aβ peptides with affinities in the micromolar range, induce structural changes in Aβ monomers and oligomers, and inhibit Aβ fibrillization. This suggests a possible link between AD and U exposure, which could be further explored by cell, animal, and epidemiological studies. General toxic mechanisms of uranyl ions could be modulation of protein folding, misfolding, and aggregation.
Uranium (U) is naturally present in ambient air, water, and soil, and depleted uranium (DU) is released into the environment via industrial and military activities. While the radiological damage from U is rather well understood, less is known about the chemical damage mechanisms, which dominate in DU. Heavy metal exposure is associated with numerous health conditions, including Alzheimer's disease (AD), the most prevalent age-related cause of dementia. The pathological hallmark of AD is the deposition of amyloid plaques, consisting mainly of amyloid-β (Aβ) peptides aggregated into amyloid fibrils in the brain. However, the toxic species in AD are likely oligomeric Aβ aggregates. Exposure to heavy metals such as Cd, Hg, Mn, and Pb is known to increase Aβ production, and these metals bind to Aβ peptides and modulate their aggregation. The possible effects of U in AD pathology have been sparsely studied. Here, we use biophysical techniques to study in vitro interactions between Aβ peptides and uranyl ions, UO , of DU. We show for the first time that uranyl ions bind to Aβ peptides with affinities in the micromolar range, induce structural changes in Aβ monomers and oligomers, and inhibit Aβ fibrillization. This suggests a possible link between AD and U exposure, which could be further explored by cell, animal, and epidemiological studies. General toxic mechanisms of uranyl ions could be modulation of protein folding, misfolding, and aggregation.
Author Berntsson, Elina
Gielnik, Maciej
Kozak, Maciej
Vosough, Faraz
Pooga, Margus
Asplund, Fanny
Barth, Andreas
Roos, Per M.
Gräslund, Astrid
Tõugu, Vello
Wärmländer, Sebastian K. T. S.
Noormägi, Andra
Palumaa, Peep
Paul, Suman
Jarvet, Jüri
Padari, Kärt
AuthorAffiliation University Healthcare Unit of Capio St. Göran Hospital
Institute of Technology
Jagiellonian University
Department of Chemistry and Biotechnology
Chemistry Section, Arrhenius Laboratories
Institute of Molecular and Cell Biology
Aarhus University
Institute of Environmental Medicine
Department of Biomedical Physics, Institute of Physics, Faculty of Physics
Department of Molecular Biology and Genetics
Adam Mickiewicz University
CellPept Sweden AB
SOLARIS National Synchrotron Radiation Centre
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CitedBy_id crossref_primary_10_1021_acschemneuro_3c00585
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Cites_doi 10.1007/978-1-4615-1863-1_10
10.1016/j.envres.2019.108927
10.1016/j.bbabio.2007.06.004
10.1016/j.envpol.2019.113070
10.1038/nature06467
10.1016/j.isci.2021.102852
10.3233/jad-2010-100705
10.1098/rspa.1955.0071
10.1074/jbc.ra120.012738
10.1126/science.8346443
10.1007/s00216-015-8835-7
10.1016/j.nbd.2022.105824
10.1080/13623699.2013.765173
10.1007/s10858-007-9176-4
10.1039/c3cc48473d
10.1021/ja310064v
10.1016/j.jenvrad.2017.03.013
10.1007/s00775-014-1131-8
10.3390/molecules24010186
10.1039/b813398k
10.1016/j.bbrc.2012.04.043
10.1016/s0091-3057(02)00772-4
10.1126/science.141.3576.154
10.1084/jem.21.1.21
10.1021/bi701213s
10.3390/biom4010252
10.3390/molecules24030405
10.1021/acs.chemrev.0c01122
10.1016/s0022-510x(98)00092-6
10.1093/oxfordjournals.rpd.a006232
10.1186/s12199-018-0706-3
10.1021/jacs.7b13623
10.1038/s41598-023-29901-5
10.1016/j.jenvrad.2019.03.009
10.5487/tr.2013.29.4.235
10.1016/j.yrtph.2014.08.012
10.1016/s0140-6736(20)32205-4
10.1038/ng0996-55
10.1016/s0021-9258(18)31395-4
10.1016/j.envres.2016.10.016
10.1007/s00775-019-01734-6
10.1016/0013-9351(83)90233-5
10.1021/ed074p1227
10.1039/c4an00918e
10.1016/j.envres.2017.04.010
10.1088/0952-4746/21/2/003
10.1007/s12011-012-9547-x
10.1007/s00775-019-01723-9
10.3390/biom10010044
10.1097/01.hp.0000149883.69107.ab
10.1002/cbic.200900321
10.1016/j.bbamem.2013.04.012
10.1039/c6cs00731g
10.1136/bmjgh-2020-004166
10.1093/rpd/ncm255
10.1021/acschemneuro.5b00325
10.1016/j.jtemb.2016.03.009
10.1002/mrc.1814
10.1074/jbc.r116.714576
10.1021/bi0358824
10.1080/13506129.2017.1304905
10.1016/j.taap.2004.09.007
10.1007/s12011-018-1527-3
10.1080/10937400903358942
10.1016/j.jsbmb.2011.12.007
10.1038/s41598-017-13759-5
10.1002/em.22283
10.1016/j.csbj.2022.10.014
10.1016/j.redox.2021.101865
10.1007/s12031-013-0038-0
10.1016/j.bpc.2021.106711
10.1039/c3cs60431d
10.1111/j.1742-4658.2008.06643.x
10.1016/j.semcdb.2020.04.002
10.2741/e819
10.1021/j100830a521
10.1289/ehp.7475
10.1016/j.taap.2015.10.022
10.1007/s00204-020-02676-8
10.1016/j.taap.2015.06.019
10.1007/s10534-014-9719-6
10.1074/jbc.m114.574947
10.1021/acschemneuro.8b00065
10.1042/bj20090379
10.1016/j.chemosphere.2018.06.059
10.1016/j.febslet.2011.03.014
10.1063/1.1731586
10.3233/jad-2003-5303
10.1007/s00294-017-0748-x
10.1016/j.bpc.2021.106700
10.1021/ja1048253
10.1016/j.bioorg.2022.106301
10.1038/sj.jes.7500551
10.1016/j.jenvrad.2018.06.004
10.1021/bi00859a010
10.1021/acs.biochem.5b01259
10.1515/reveh.2005.20.3.177
10.1016/j.jmb.2019.01.018
10.1016/j.scitotenv.2013.11.109
10.1002/alz.12328
10.1016/j.xcrp.2020.100014
10.1021/ic7018633
10.1039/c2mt20113e
10.1016/j.bbapap.2018.11.005
10.3233/jad-160427
10.1111/j.1471-4159.2005.03407.x
10.1016/j.jinorgbio.2012.11.005
10.1021/cn300170x
10.1080/15287390701550987
10.1021/acschemneuro.0c00642
10.1002/em.22281
10.1016/j.neuron.2009.06.026
10.1002/jat.841
10.1186/s41021-015-0019-3
10.1016/j.toxlet.2015.05.006
10.1038/s41598-018-33935-5
10.1002/chem.202004484
10.1259/bjr.74.884.740677
10.12659/MSM.934077
10.1016/s0006-291x(84)80190-4
10.1007/bf01257128
10.1016/j.bbrc.2019.01.120
10.1016/j.cis.2012.08.003
10.1021/acs.jpcb.6b10797
10.3389/fnagi.2022.870517
10.1021/ac302629u
10.1080/13506120500106958
10.1016/j.tox.2015.08.004
10.1016/j.bbrc.2008.05.052
10.1186/1750-1326-1-5
10.1038/nchem.1856
10.1111/j.1742-4658.2006.05563.x
10.1128/aem.00538-16
10.1039/c8cs00034d
10.1021/ic4003059
10.1515/intox-2015-0024
10.2174/0929867324666170426102343
10.1007/s12035-019-1563-9
10.1017/s0033583502003815
10.1016/j.jsb.2005.09.004
10.1002/chem.201301535
10.3390/life11010028
10.1111/j.1745-6584.2004.tb02692.x
10.3233/jad-181144
10.1021/acs.estlett.5b00174
10.18388/abp.2020_5493
10.1016/j.envres.2005.12.010
10.1002/ijc.20680
10.1039/c6cp03469a
10.1002/ana.25918
10.1016/j.jenvrad.2019.03.004
10.1371/journal.pcbi.1000663
10.1093/toxsci/kfu208
10.1021/acsomega.2c02254
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Issue 15
Keywords neurodegeneration
metal−protein binding
amyloid aggregation
heavy metal toxicity
Alzheimer’s disease
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References ref45/cit45
ref99/cit99
ref3/cit3
ref81/cit81
ref16/cit16
ref52/cit52
ref114/cit114
ref23/cit23
ref115/cit115
ref116/cit116
ref111/cit111
ref2/cit2
ref112/cit112
ref77/cit77
ref113/cit113
Mirderikvand N. (ref88/cit88) 2014; 13
ref71/cit71
ref117/cit117
ref20/cit20
ref48/cit48
ref118/cit118
ref74/cit74
ref119/cit119
ref10/cit10
ref35/cit35
ref89/cit89
ref19/cit19
ref93/cit93
ref42/cit42
ref96/cit96
ref107/cit107
ref120/cit120
ref109/cit109
ref13/cit13
ref122/cit122
ref105/cit105
ref61/cit61
ref67/cit67
Agency for Toxic Substances and Disease Registry (ref56/cit56) 2013
ref38/cit38
ref128/cit128
ref90/cit90
ref124/cit124
ref64/cit64
ref126/cit126
ref54/cit54
ref6/cit6
ref18/cit18
ref136/cit136
ref137/cit137
ref65/cit65
ref97/cit97
ref101/cit101
ref11/cit11
ref102/cit102
ref29/cit29
ref76/cit76
ref86/cit86
ref32/cit32
ref5/cit5
ref43/cit43
ref80/cit80
ref133/cit133
ref28/cit28
ref132/cit132
ref91/cit91
Kuzmic P. (ref160/cit160) 2015
ref148/cit148
ref55/cit55
ref144/cit144
ref12/cit12
ref66/cit66
ref22/cit22
ref121/cit121
ref33/cit33
ref87/cit87
ref106/cit106
ref140/cit140
ref129/cit129
ref44/cit44
ref70/cit70
ref98/cit98
ref125/cit125
ref9/cit9
ref152/cit152
ref153/cit153
ref154/cit154
ref27/cit27
ref150/cit150
ref63/cit63
ref151/cit151
ref159/cit159
ref92/cit92
ref155/cit155
ref156/cit156
ref157/cit157
ref158/cit158
ref8/cit8
ref31/cit31
ref59/cit59
ref85/cit85
ref34/cit34
ref37/cit37
ref60/cit60
ref17/cit17
Nordberg G. (ref39/cit39) 2021
ref82/cit82
ref147/cit147
ref143/cit143
ref53/cit53
ref145/cit145
ref21/cit21
ref149/cit149
ref162/cit162
ref46/cit46
ref49/cit49
ref75/cit75
ref24/cit24
ref141/cit141
ref50/cit50
ref78/cit78
ref36/cit36
ref83/cit83
ref138/cit138
ref79/cit79
ref139/cit139
ref100/cit100
Mutter J. (ref110/cit110) 2004; 25
ref25/cit25
ref103/cit103
ref72/cit72
ref14/cit14
ref57/cit57
ref51/cit51
ref134/cit134
ref135/cit135
ref40/cit40
ref68/cit68
ref94/cit94
ref130/cit130
ref131/cit131
ref146/cit146
ref26/cit26
ref161/cit161
ref142/cit142
ref73/cit73
ref69/cit69
ref15/cit15
ref62/cit62
ref41/cit41
ref58/cit58
ref95/cit95
ref108/cit108
ref104/cit104
ref4/cit4
ref30/cit30
ref47/cit47
ref84/cit84
ref127/cit127
ref1/cit1
ref123/cit123
ref7/cit7
References_xml – ident: ref134/cit134
  doi: 10.1007/978-1-4615-1863-1_10
– ident: ref52/cit52
  doi: 10.1016/j.envres.2019.108927
– ident: ref133/cit133
  doi: 10.1016/j.bbabio.2007.06.004
– ident: ref64/cit64
  doi: 10.1016/j.envpol.2019.113070
– ident: ref144/cit144
  doi: 10.1038/nature06467
– ident: ref143/cit143
  doi: 10.1016/j.isci.2021.102852
– volume-title: History, Variants and Usage of the “Morrison Equation” in Enzyme Inhibition Kinetics
  year: 2015
  ident: ref160/cit160
  contributor:
    fullname: Kuzmic P.
– ident: ref105/cit105
  doi: 10.3233/jad-2010-100705
– ident: ref100/cit100
  doi: 10.1098/rspa.1955.0071
– ident: ref30/cit30
  doi: 10.1074/jbc.ra120.012738
– ident: ref108/cit108
  doi: 10.1126/science.8346443
– ident: ref84/cit84
  doi: 10.1007/s00216-015-8835-7
– ident: ref114/cit114
  doi: 10.1016/j.nbd.2022.105824
– volume-title: Toxicological Profile for Uranium
  year: 2013
  ident: ref56/cit56
  contributor:
    fullname: Agency for Toxic Substances and Disease Registry
– ident: ref69/cit69
  doi: 10.1080/13623699.2013.765173
– ident: ref19/cit19
  doi: 10.1007/s10858-007-9176-4
– ident: ref38/cit38
  doi: 10.1039/c3cc48473d
– ident: ref9/cit9
  doi: 10.1021/ja310064v
– ident: ref58/cit58
  doi: 10.1016/j.jenvrad.2017.03.013
– ident: ref18/cit18
  doi: 10.1007/s00775-014-1131-8
– ident: ref138/cit138
  doi: 10.3390/molecules24010186
– ident: ref141/cit141
  doi: 10.1039/b813398k
– ident: ref119/cit119
  doi: 10.1016/j.bbrc.2012.04.043
– ident: ref93/cit93
  doi: 10.1016/s0091-3057(02)00772-4
– ident: ref102/cit102
  doi: 10.1126/science.141.3576.154
– ident: ref81/cit81
  doi: 10.1084/jem.21.1.21
– ident: ref153/cit153
  doi: 10.1021/bi701213s
– ident: ref42/cit42
  doi: 10.3390/biom4010252
– ident: ref124/cit124
  doi: 10.3390/molecules24030405
– ident: ref13/cit13
  doi: 10.1021/acs.chemrev.0c01122
– ident: ref33/cit33
  doi: 10.1016/s0022-510x(98)00092-6
– ident: ref50/cit50
  doi: 10.1093/oxfordjournals.rpd.a006232
– ident: ref71/cit71
  doi: 10.1186/s12199-018-0706-3
– ident: ref26/cit26
  doi: 10.1021/jacs.7b13623
– ident: ref118/cit118
  doi: 10.1038/s41598-023-29901-5
– ident: ref97/cit97
  doi: 10.1016/j.jenvrad.2019.03.009
– ident: ref46/cit46
  doi: 10.5487/tr.2013.29.4.235
– ident: ref82/cit82
  doi: 10.1016/j.yrtph.2014.08.012
– ident: ref1/cit1
  doi: 10.1016/s0140-6736(20)32205-4
– ident: ref109/cit109
  doi: 10.1038/ng0996-55
– ident: ref130/cit130
  doi: 10.1016/s0021-9258(18)31395-4
– ident: ref66/cit66
  doi: 10.1016/j.envres.2016.10.016
– ident: ref128/cit128
  doi: 10.1007/s00775-019-01734-6
– ident: ref80/cit80
  doi: 10.1016/0013-9351(83)90233-5
– ident: ref152/cit152
  doi: 10.1021/ed074p1227
– ident: ref162/cit162
  doi: 10.1039/c4an00918e
– ident: ref78/cit78
  doi: 10.1016/j.envres.2017.04.010
– ident: ref70/cit70
  doi: 10.1088/0952-4746/21/2/003
– ident: ref91/cit91
  doi: 10.1007/s12011-012-9547-x
– ident: ref36/cit36
  doi: 10.1007/s00775-019-01723-9
– ident: ref47/cit47
  doi: 10.3390/biom10010044
– ident: ref74/cit74
  doi: 10.1097/01.hp.0000149883.69107.ab
– ident: ref149/cit149
  doi: 10.1002/cbic.200900321
– ident: ref137/cit137
  doi: 10.1016/j.bbamem.2013.04.012
– ident: ref11/cit11
  doi: 10.1039/c6cs00731g
– ident: ref65/cit65
  doi: 10.1136/bmjgh-2020-004166
– ident: ref86/cit86
  doi: 10.1093/rpd/ncm255
– ident: ref25/cit25
  doi: 10.1021/acschemneuro.5b00325
– ident: ref140/cit140
  doi: 10.1016/j.jtemb.2016.03.009
– ident: ref157/cit157
  doi: 10.1002/mrc.1814
– ident: ref24/cit24
  doi: 10.1074/jbc.r116.714576
– ident: ref35/cit35
  doi: 10.1021/bi0358824
– ident: ref116/cit116
  doi: 10.1080/13506129.2017.1304905
– ident: ref40/cit40
  doi: 10.1016/j.taap.2004.09.007
– ident: ref67/cit67
  doi: 10.1007/s12011-018-1527-3
– ident: ref87/cit87
  doi: 10.1080/10937400903358942
– ident: ref104/cit104
  doi: 10.1016/j.jsbmb.2011.12.007
– ident: ref3/cit3
  doi: 10.1038/s41598-017-13759-5
– ident: ref62/cit62
  doi: 10.1002/em.22283
– ident: ref23/cit23
  doi: 10.1016/j.csbj.2022.10.014
– ident: ref107/cit107
  doi: 10.1016/j.redox.2021.101865
– ident: ref103/cit103
  doi: 10.1007/s12031-013-0038-0
– ident: ref14/cit14
  doi: 10.1016/j.bpc.2021.106711
– ident: ref147/cit147
  doi: 10.1039/c3cs60431d
– ident: ref20/cit20
  doi: 10.1111/j.1742-4658.2008.06643.x
– ident: ref17/cit17
  doi: 10.1016/j.semcdb.2020.04.002
– ident: ref76/cit76
– ident: ref106/cit106
  doi: 10.2741/e819
– ident: ref154/cit154
  doi: 10.1021/j100830a521
– ident: ref83/cit83
  doi: 10.1289/ehp.7475
– ident: ref95/cit95
  doi: 10.1016/j.taap.2015.10.022
– ident: ref53/cit53
  doi: 10.1007/s00204-020-02676-8
– ident: ref77/cit77
– ident: ref94/cit94
  doi: 10.1016/j.taap.2015.06.019
– ident: ref48/cit48
  doi: 10.1007/s10534-014-9719-6
– ident: ref22/cit22
  doi: 10.1074/jbc.m114.574947
– ident: ref125/cit125
  doi: 10.1021/acschemneuro.8b00065
– ident: ref136/cit136
  doi: 10.1042/bj20090379
– volume: 25
  start-page: 331
  year: 2004
  ident: ref110/cit110
  publication-title: Neuroendocrinol. Lett.
  contributor:
    fullname: Mutter J.
– ident: ref150/cit150
  doi: 10.1016/j.chemosphere.2018.06.059
– ident: ref159/cit159
  doi: 10.1016/j.febslet.2011.03.014
– ident: ref99/cit99
  doi: 10.1063/1.1731586
– ident: ref111/cit111
  doi: 10.3233/jad-2003-5303
– ident: ref43/cit43
  doi: 10.1007/s00294-017-0748-x
– ident: ref148/cit148
  doi: 10.1016/j.bpc.2021.106700
– ident: ref101/cit101
– ident: ref120/cit120
  doi: 10.1021/ja1048253
– ident: ref29/cit29
  doi: 10.1016/j.bioorg.2022.106301
– ident: ref57/cit57
  doi: 10.1038/sj.jes.7500551
– ident: ref59/cit59
  doi: 10.1016/j.jenvrad.2018.06.004
– ident: ref155/cit155
  doi: 10.1021/bi00859a010
– ident: ref158/cit158
  doi: 10.1021/acs.biochem.5b01259
– ident: ref55/cit55
  doi: 10.1515/reveh.2005.20.3.177
– ident: ref31/cit31
  doi: 10.1016/j.jmb.2019.01.018
– ident: ref75/cit75
  doi: 10.1016/j.scitotenv.2013.11.109
– ident: ref2/cit2
  doi: 10.1002/alz.12328
– ident: ref27/cit27
  doi: 10.1016/j.xcrp.2020.100014
– ident: ref145/cit145
  doi: 10.1021/ic7018633
– ident: ref37/cit37
  doi: 10.1039/c2mt20113e
– volume: 13
  start-page: 199
  year: 2014
  ident: ref88/cit88
  publication-title: Iran. J. Pharm. Res.
  contributor:
    fullname: Mirderikvand N.
– ident: ref126/cit126
  doi: 10.1016/j.bbapap.2018.11.005
– ident: ref122/cit122
  doi: 10.3233/jad-160427
– ident: ref131/cit131
  doi: 10.1111/j.1471-4159.2005.03407.x
– ident: ref121/cit121
  doi: 10.1016/j.jinorgbio.2012.11.005
– ident: ref28/cit28
  doi: 10.1021/cn300170x
– ident: ref92/cit92
  doi: 10.1080/15287390701550987
– ident: ref132/cit132
  doi: 10.1021/acschemneuro.0c00642
– ident: ref61/cit61
  doi: 10.1002/em.22281
– ident: ref112/cit112
  doi: 10.1016/j.neuron.2009.06.026
– ident: ref60/cit60
  doi: 10.1002/jat.841
– ident: ref79/cit79
  doi: 10.1186/s41021-015-0019-3
– ident: ref85/cit85
  doi: 10.1016/j.toxlet.2015.05.006
– ident: ref127/cit127
  doi: 10.1038/s41598-018-33935-5
– ident: ref32/cit32
  doi: 10.1002/chem.202004484
– ident: ref68/cit68
  doi: 10.1259/bjr.74.884.740677
– ident: ref7/cit7
  doi: 10.12659/MSM.934077
– ident: ref15/cit15
  doi: 10.1016/s0006-291x(84)80190-4
– ident: ref49/cit49
  doi: 10.1007/bf01257128
– ident: ref129/cit129
  doi: 10.1016/j.bbrc.2019.01.120
– ident: ref156/cit156
  doi: 10.1016/j.cis.2012.08.003
– ident: ref151/cit151
  doi: 10.1021/acs.jpcb.6b10797
– ident: ref10/cit10
  doi: 10.3389/fnagi.2022.870517
– ident: ref123/cit123
  doi: 10.1021/ac302629u
– ident: ref161/cit161
  doi: 10.1080/13506120500106958
– ident: ref51/cit51
  doi: 10.1016/j.tox.2015.08.004
– ident: ref41/cit41
  doi: 10.1016/j.bbrc.2008.05.052
– ident: ref16/cit16
  doi: 10.1186/1750-1326-1-5
– ident: ref98/cit98
  doi: 10.1038/nchem.1856
– ident: ref117/cit117
  doi: 10.1111/j.1742-4658.2006.05563.x
– ident: ref96/cit96
  doi: 10.1128/aem.00538-16
– ident: ref21/cit21
  doi: 10.1039/c8cs00034d
– ident: ref142/cit142
  doi: 10.1021/ic4003059
– ident: ref44/cit44
  doi: 10.1515/intox-2015-0024
– ident: ref54/cit54
  doi: 10.2174/0929867324666170426102343
– ident: ref5/cit5
  doi: 10.1007/s12035-019-1563-9
– ident: ref135/cit135
  doi: 10.1017/s0033583502003815
– ident: ref34/cit34
  doi: 10.1016/j.jsb.2005.09.004
– ident: ref8/cit8
  doi: 10.1002/chem.201301535
– ident: ref12/cit12
  doi: 10.3390/life11010028
– ident: ref73/cit73
  doi: 10.1111/j.1745-6584.2004.tb02692.x
– ident: ref6/cit6
  doi: 10.3233/jad-181144
– ident: ref72/cit72
  doi: 10.1021/acs.estlett.5b00174
– ident: ref139/cit139
  doi: 10.18388/abp.2020_5493
– ident: ref90/cit90
  doi: 10.1016/j.envres.2005.12.010
– ident: ref89/cit89
  doi: 10.1002/ijc.20680
– ident: ref146/cit146
  doi: 10.1039/c6cp03469a
– ident: ref4/cit4
  doi: 10.1002/ana.25918
– ident: ref63/cit63
  doi: 10.1016/j.jenvrad.2019.03.004
– ident: ref113/cit113
  doi: 10.1371/journal.pcbi.1000663
– ident: ref45/cit45
  doi: 10.1093/toxsci/kfu208
– ident: ref115/cit115
  doi: 10.1021/acsomega.2c02254
– volume-title: Handbook on the Toxicology of Metals
  year: 2021
  ident: ref39/cit39
  contributor:
    fullname: Nordberg G.
SSID ssj0069086
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Snippet Uranium (U) is naturally present in ambient air, water, and soil, and depleted uranium (DU) is released into the environment via industrial and military...
Uranium (U) is naturally present in ambient air, water, and soil, and depleted uranium (DU) is released into the environment via industrial and military...
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SourceType Open Access Repository
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SubjectTerms Alzheimer Disease - metabolism
Alzheimer's disease
Amyloid
amyloid aggregation
Amyloid beta-Peptides - metabolism
Animals
heavy metal toxicity
Ions - chemistry
Medicin och hälsovetenskap
metal-protein binding
neurodegeneration
Uranium
Title Characterization of Uranyl (UO2 2+) Ion Binding to Amyloid Beta (Aβ) Peptides: Effects on Aβ Structure and Aggregation
URI http://dx.doi.org/10.1021/acschemneuro.3c00130
https://www.ncbi.nlm.nih.gov/pubmed/37487115
https://search.proquest.com/docview/2841880606
https://pubmed.ncbi.nlm.nih.gov/PMC10401651
https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-221233
http://kipublications.ki.se/Default.aspx?queryparsed=id:153234755
Volume 14
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