Electrochemical studies of tau protein-iron interactions—Potential implications for Alzheimer’s Disease

[Display omitted] Tau, a family of microtubule-associated protein (MAP) that exists in six isoforms, is involved in the etiology of Alzheimer’s and upon hypophosphorylation gives rise to neurofibrillary tangles (NFTs) inside neurons. Here, we report the results of an electrochemical investigation in...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Electrochimica acta 2017-05, Vol.236, p.384-393
Hauptverfasser: Ahmadi, Soha, Ebralidze, Iraklii I., She, Zhe, Kraatz, Heinz-Bernhard
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 393
container_issue
container_start_page 384
container_title Electrochimica acta
container_volume 236
creator Ahmadi, Soha
Ebralidze, Iraklii I.
She, Zhe
Kraatz, Heinz-Bernhard
description [Display omitted] Tau, a family of microtubule-associated protein (MAP) that exists in six isoforms, is involved in the etiology of Alzheimer’s and upon hypophosphorylation gives rise to neurofibrillary tangles (NFTs) inside neurons. Here, we report the results of an electrochemical investigation into the interaction of Fe(II) and Fe(III) with surface-supported tau (Tau-410, 2N3R). Changes in current density and impedance changes were used to monitor metal-tau interactions and tau-tau interactions. Our detailed electrochemical studies of surface-supported tau protein is supported by X-ray photoelectron spectroscopy (XPS) and by measurement of interactions in solution by circular dichroism (CD) spectroscopy. In addition, we include the effects of tau phosphorylation on the interactions with Fe(II) and Fe(III). Our results clearly demonstrate that a) Fe(II) and Fe(III) bind to the tau protein, b) structural changes occur to tau upon metal binding, c) Fe(II) shows a more pronounced effect, d) phosphorylation affects the metal ion complexation and e) tau-tau interactions are mediated by Fe(II).
doi_str_mv 10.1016/j.electacta.2017.03.175
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_1931715398</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0013468617306850</els_id><sourcerecordid>1931715398</sourcerecordid><originalsourceid>FETCH-LOGICAL-c434t-bc2eba10c1b1a6a950d2a04f2d4ddde80b363885d9f2d57f30fc16b219788aff3</originalsourceid><addsrcrecordid>eNqFkM1KxDAQx4MouH48gwXPrZOmbdLjsn6CoAc9hzSZsFm7zZp0BT35EF58PZ_ErCtehYGBmf9vPv6EnFAoKNDmbFFgj3pUKYoSKC-AFZTXO2RCBWc5E3W7SyYAlOVVI5p9chDjAgB4w2FCni42cPB6jkunVZ_FcW0cxszbbFTrbBX8iG7IXfBD5oYRQ1rk_BC_3j_uU2sYXYLcctUn-qeRWR-yaf82R7fE8PX-GbNzF1FFPCJ7VvURj3_zIXm8vHiYXee3d1c3s-ltritWjXmnS-wUBU07qhrV1mBKBZUtTWWMQQEda5gQtWlTqeaWgdW06UraciGUteyQnG7npuOf1xhHufDrMKSVkraMclqzViQV36p08DEGtHIV3FKFV0lBbpyVC_nnrNw4K4HJ5Gwip1sS0xMvDoOM2uGg0biQ9NJ49--MbzZZixU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1931715398</pqid></control><display><type>article</type><title>Electrochemical studies of tau protein-iron interactions—Potential implications for Alzheimer’s Disease</title><source>Access via ScienceDirect (Elsevier)</source><creator>Ahmadi, Soha ; Ebralidze, Iraklii I. ; She, Zhe ; Kraatz, Heinz-Bernhard</creator><creatorcontrib>Ahmadi, Soha ; Ebralidze, Iraklii I. ; She, Zhe ; Kraatz, Heinz-Bernhard</creatorcontrib><description>[Display omitted] Tau, a family of microtubule-associated protein (MAP) that exists in six isoforms, is involved in the etiology of Alzheimer’s and upon hypophosphorylation gives rise to neurofibrillary tangles (NFTs) inside neurons. Here, we report the results of an electrochemical investigation into the interaction of Fe(II) and Fe(III) with surface-supported tau (Tau-410, 2N3R). Changes in current density and impedance changes were used to monitor metal-tau interactions and tau-tau interactions. Our detailed electrochemical studies of surface-supported tau protein is supported by X-ray photoelectron spectroscopy (XPS) and by measurement of interactions in solution by circular dichroism (CD) spectroscopy. In addition, we include the effects of tau phosphorylation on the interactions with Fe(II) and Fe(III). Our results clearly demonstrate that a) Fe(II) and Fe(III) bind to the tau protein, b) structural changes occur to tau upon metal binding, c) Fe(II) shows a more pronounced effect, d) phosphorylation affects the metal ion complexation and e) tau-tau interactions are mediated by Fe(II).</description><identifier>ISSN: 0013-4686</identifier><identifier>EISSN: 1873-3859</identifier><identifier>DOI: 10.1016/j.electacta.2017.03.175</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Alzheimer's disease ; Alzheimer’s ; Current density ; Dichroism ; electrochemistry ; Etiology ; Iron ; metal interactions ; Phosphorylation ; Spectroscopic analysis ; Spectrum analysis ; tau ; X ray photoelectron spectroscopy</subject><ispartof>Electrochimica acta, 2017-05, Vol.236, p.384-393</ispartof><rights>2017 Elsevier Ltd</rights><rights>Copyright Elsevier BV May 10, 2017</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-bc2eba10c1b1a6a950d2a04f2d4ddde80b363885d9f2d57f30fc16b219788aff3</citedby><cites>FETCH-LOGICAL-c434t-bc2eba10c1b1a6a950d2a04f2d4ddde80b363885d9f2d57f30fc16b219788aff3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.electacta.2017.03.175$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids></links><search><creatorcontrib>Ahmadi, Soha</creatorcontrib><creatorcontrib>Ebralidze, Iraklii I.</creatorcontrib><creatorcontrib>She, Zhe</creatorcontrib><creatorcontrib>Kraatz, Heinz-Bernhard</creatorcontrib><title>Electrochemical studies of tau protein-iron interactions—Potential implications for Alzheimer’s Disease</title><title>Electrochimica acta</title><description>[Display omitted] Tau, a family of microtubule-associated protein (MAP) that exists in six isoforms, is involved in the etiology of Alzheimer’s and upon hypophosphorylation gives rise to neurofibrillary tangles (NFTs) inside neurons. Here, we report the results of an electrochemical investigation into the interaction of Fe(II) and Fe(III) with surface-supported tau (Tau-410, 2N3R). Changes in current density and impedance changes were used to monitor metal-tau interactions and tau-tau interactions. Our detailed electrochemical studies of surface-supported tau protein is supported by X-ray photoelectron spectroscopy (XPS) and by measurement of interactions in solution by circular dichroism (CD) spectroscopy. In addition, we include the effects of tau phosphorylation on the interactions with Fe(II) and Fe(III). Our results clearly demonstrate that a) Fe(II) and Fe(III) bind to the tau protein, b) structural changes occur to tau upon metal binding, c) Fe(II) shows a more pronounced effect, d) phosphorylation affects the metal ion complexation and e) tau-tau interactions are mediated by Fe(II).</description><subject>Alzheimer's disease</subject><subject>Alzheimer’s</subject><subject>Current density</subject><subject>Dichroism</subject><subject>electrochemistry</subject><subject>Etiology</subject><subject>Iron</subject><subject>metal interactions</subject><subject>Phosphorylation</subject><subject>Spectroscopic analysis</subject><subject>Spectrum analysis</subject><subject>tau</subject><subject>X ray photoelectron spectroscopy</subject><issn>0013-4686</issn><issn>1873-3859</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNqFkM1KxDAQx4MouH48gwXPrZOmbdLjsn6CoAc9hzSZsFm7zZp0BT35EF58PZ_ErCtehYGBmf9vPv6EnFAoKNDmbFFgj3pUKYoSKC-AFZTXO2RCBWc5E3W7SyYAlOVVI5p9chDjAgB4w2FCni42cPB6jkunVZ_FcW0cxszbbFTrbBX8iG7IXfBD5oYRQ1rk_BC_3j_uU2sYXYLcctUn-qeRWR-yaf82R7fE8PX-GbNzF1FFPCJ7VvURj3_zIXm8vHiYXee3d1c3s-ltritWjXmnS-wUBU07qhrV1mBKBZUtTWWMQQEda5gQtWlTqeaWgdW06UraciGUteyQnG7npuOf1xhHufDrMKSVkraMclqzViQV36p08DEGtHIV3FKFV0lBbpyVC_nnrNw4K4HJ5Gwip1sS0xMvDoOM2uGg0biQ9NJ49--MbzZZixU</recordid><startdate>20170510</startdate><enddate>20170510</enddate><creator>Ahmadi, Soha</creator><creator>Ebralidze, Iraklii I.</creator><creator>She, Zhe</creator><creator>Kraatz, Heinz-Bernhard</creator><general>Elsevier Ltd</general><general>Elsevier BV</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20170510</creationdate><title>Electrochemical studies of tau protein-iron interactions—Potential implications for Alzheimer’s Disease</title><author>Ahmadi, Soha ; Ebralidze, Iraklii I. ; She, Zhe ; Kraatz, Heinz-Bernhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-bc2eba10c1b1a6a950d2a04f2d4ddde80b363885d9f2d57f30fc16b219788aff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Alzheimer's disease</topic><topic>Alzheimer’s</topic><topic>Current density</topic><topic>Dichroism</topic><topic>electrochemistry</topic><topic>Etiology</topic><topic>Iron</topic><topic>metal interactions</topic><topic>Phosphorylation</topic><topic>Spectroscopic analysis</topic><topic>Spectrum analysis</topic><topic>tau</topic><topic>X ray photoelectron spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ahmadi, Soha</creatorcontrib><creatorcontrib>Ebralidze, Iraklii I.</creatorcontrib><creatorcontrib>She, Zhe</creatorcontrib><creatorcontrib>Kraatz, Heinz-Bernhard</creatorcontrib><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Electrochimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ahmadi, Soha</au><au>Ebralidze, Iraklii I.</au><au>She, Zhe</au><au>Kraatz, Heinz-Bernhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electrochemical studies of tau protein-iron interactions—Potential implications for Alzheimer’s Disease</atitle><jtitle>Electrochimica acta</jtitle><date>2017-05-10</date><risdate>2017</risdate><volume>236</volume><spage>384</spage><epage>393</epage><pages>384-393</pages><issn>0013-4686</issn><eissn>1873-3859</eissn><abstract>[Display omitted] Tau, a family of microtubule-associated protein (MAP) that exists in six isoforms, is involved in the etiology of Alzheimer’s and upon hypophosphorylation gives rise to neurofibrillary tangles (NFTs) inside neurons. Here, we report the results of an electrochemical investigation into the interaction of Fe(II) and Fe(III) with surface-supported tau (Tau-410, 2N3R). Changes in current density and impedance changes were used to monitor metal-tau interactions and tau-tau interactions. Our detailed electrochemical studies of surface-supported tau protein is supported by X-ray photoelectron spectroscopy (XPS) and by measurement of interactions in solution by circular dichroism (CD) spectroscopy. In addition, we include the effects of tau phosphorylation on the interactions with Fe(II) and Fe(III). Our results clearly demonstrate that a) Fe(II) and Fe(III) bind to the tau protein, b) structural changes occur to tau upon metal binding, c) Fe(II) shows a more pronounced effect, d) phosphorylation affects the metal ion complexation and e) tau-tau interactions are mediated by Fe(II).</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><doi>10.1016/j.electacta.2017.03.175</doi><tpages>10</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0013-4686
ispartof Electrochimica acta, 2017-05, Vol.236, p.384-393
issn 0013-4686
1873-3859
language eng
recordid cdi_proquest_journals_1931715398
source Access via ScienceDirect (Elsevier)
subjects Alzheimer's disease
Alzheimer’s
Current density
Dichroism
electrochemistry
Etiology
Iron
metal interactions
Phosphorylation
Spectroscopic analysis
Spectrum analysis
tau
X ray photoelectron spectroscopy
title Electrochemical studies of tau protein-iron interactions—Potential implications for Alzheimer’s Disease
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-05T11%3A55%3A49IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Electrochemical%20studies%20of%20tau%20protein-iron%20interactions%E2%80%94Potential%20implications%20for%20Alzheimer%E2%80%99s%20Disease&rft.jtitle=Electrochimica%20acta&rft.au=Ahmadi,%20Soha&rft.date=2017-05-10&rft.volume=236&rft.spage=384&rft.epage=393&rft.pages=384-393&rft.issn=0013-4686&rft.eissn=1873-3859&rft_id=info:doi/10.1016/j.electacta.2017.03.175&rft_dat=%3Cproquest_cross%3E1931715398%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1931715398&rft_id=info:pmid/&rft_els_id=S0013468617306850&rfr_iscdi=true