Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry
There is an ongoing debate regarding the culprits of cytotoxicity associated with amyloid disorders. Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce cytotoxicity. To investigate membrane disruptio...
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| Veröffentlicht in: | PloS one 2015-07, Vol.10 (7), p.e0132309 |
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| creator | Smith, Rachel A S Nabok, Aleksey Blakeman, Ben J F Xue, Wei-Feng Abell, Benjamin Smith, David P |
| description | There is an ongoing debate regarding the culprits of cytotoxicity associated with amyloid disorders. Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce cytotoxicity. To investigate membrane disruption and cytotoxic effects associated with intact and fragmented fibrils, the novel in situ spectroscopic technique of Total Internal Reflection Ellipsometry (TIRE) was used. Fibril lipid interactions were monitored using natively derived whole cell membranes as a model of the in vivo environment. We show that fragmented fibrils have an increased ability to disrupt these natively derived membranes by causing a loss of material from the deposited surface when compared with unfragmented fibrils. This effect was corroborated by observations of membrane disruption in live cells, and by dye release assay using synthetic liposomes. Through these studies we demonstrate the use of TIRE for the analysis of protein-lipid interactions on natively derived lipid surfaces, and provide an explanation on how amyloid fibrils can cause a toxic gain of function, while entangled amyloid plaques exert minimal biological activity. |
| doi_str_mv | 10.1371/journal.pone.0132309 |
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Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce cytotoxicity. To investigate membrane disruption and cytotoxic effects associated with intact and fragmented fibrils, the novel in situ spectroscopic technique of Total Internal Reflection Ellipsometry (TIRE) was used. Fibril lipid interactions were monitored using natively derived whole cell membranes as a model of the in vivo environment. We show that fragmented fibrils have an increased ability to disrupt these natively derived membranes by causing a loss of material from the deposited surface when compared with unfragmented fibrils. This effect was corroborated by observations of membrane disruption in live cells, and by dye release assay using synthetic liposomes. Through these studies we demonstrate the use of TIRE for the analysis of protein-lipid interactions on natively derived lipid surfaces, and provide an explanation on how amyloid fibrils can cause a toxic gain of function, while entangled amyloid plaques exert minimal biological activity.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0132309</identifier><identifier>PMID: 26172440</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>alpha-Synuclein - metabolism ; alpha-Synuclein - toxicity ; Alzheimer's disease ; Alzheimers disease ; Amyloid - metabolism ; Amyloid - toxicity ; Amyloid beta-Peptides - metabolism ; Amyloid beta-Peptides - toxicity ; Animals ; Biocompatibility ; Biological activity ; Biomedical research ; Biosensors ; Cell Line, Tumor ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Cell membranes ; Cytotoxicity ; Dye releases ; E coli ; Ellipsometry ; Environmental monitoring ; Fibrils ; Humans ; Lipids ; Liposomes ; Liposomes - metabolism ; Membranes ; Molecular structure ; Muramidase - metabolism ; Muramidase - toxicity ; Mutation ; Oligomers ; Optical Phenomena ; Peptide Fragments - metabolism ; Peptide Fragments - toxicity ; Peptides ; Protein Binding ; Proteins ; Senile plaques ; Studies ; Toxicity</subject><ispartof>PloS one, 2015-07, Vol.10 (7), p.e0132309</ispartof><rights>2015 Smith et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Smith et al 2015 Smith et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-dddd8c8d7c7afb0f4879333816b3ceecdaced66e0ea416e727a8a78db03038853</citedby><cites>FETCH-LOGICAL-c526t-dddd8c8d7c7afb0f4879333816b3ceecdaced66e0ea416e727a8a78db03038853</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4501548/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4501548/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26172440$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Leonenko, Zoya</contributor><creatorcontrib>Smith, Rachel A S</creatorcontrib><creatorcontrib>Nabok, Aleksey</creatorcontrib><creatorcontrib>Blakeman, Ben J F</creatorcontrib><creatorcontrib>Xue, Wei-Feng</creatorcontrib><creatorcontrib>Abell, Benjamin</creatorcontrib><creatorcontrib>Smith, David P</creatorcontrib><title>Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>There is an ongoing debate regarding the culprits of cytotoxicity associated with amyloid disorders. Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce cytotoxicity. To investigate membrane disruption and cytotoxic effects associated with intact and fragmented fibrils, the novel in situ spectroscopic technique of Total Internal Reflection Ellipsometry (TIRE) was used. Fibril lipid interactions were monitored using natively derived whole cell membranes as a model of the in vivo environment. We show that fragmented fibrils have an increased ability to disrupt these natively derived membranes by causing a loss of material from the deposited surface when compared with unfragmented fibrils. This effect was corroborated by observations of membrane disruption in live cells, and by dye release assay using synthetic liposomes. Through these studies we demonstrate the use of TIRE for the analysis of protein-lipid interactions on natively derived lipid surfaces, and provide an explanation on how amyloid fibrils can cause a toxic gain of function, while entangled amyloid plaques exert minimal biological activity.</description><subject>alpha-Synuclein - metabolism</subject><subject>alpha-Synuclein - toxicity</subject><subject>Alzheimer's disease</subject><subject>Alzheimers disease</subject><subject>Amyloid - metabolism</subject><subject>Amyloid - toxicity</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Amyloid beta-Peptides - toxicity</subject><subject>Animals</subject><subject>Biocompatibility</subject><subject>Biological activity</subject><subject>Biomedical research</subject><subject>Biosensors</subject><subject>Cell Line, Tumor</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - metabolism</subject><subject>Cell membranes</subject><subject>Cytotoxicity</subject><subject>Dye releases</subject><subject>E coli</subject><subject>Ellipsometry</subject><subject>Environmental monitoring</subject><subject>Fibrils</subject><subject>Humans</subject><subject>Lipids</subject><subject>Liposomes</subject><subject>Liposomes - metabolism</subject><subject>Membranes</subject><subject>Molecular structure</subject><subject>Muramidase - metabolism</subject><subject>Muramidase - toxicity</subject><subject>Mutation</subject><subject>Oligomers</subject><subject>Optical Phenomena</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Fragments - toxicity</subject><subject>Peptides</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Senile plaques</subject><subject>Studies</subject><subject>Toxicity</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNp1kk9v3CAQxa2qUZOm-QZVi9TzboCxAV8qrfJ3pbS9pKccEIZxygqbLXij-tvX6TpRcigXRvDm90bwiuIjo0sGkp1u4i71Jiy3scclZcCB1m-KI1YDXwhO4e2L-rB4n_OG0gqUEO-KQy6Y5GVJj4q71cQYs88ktuQ2_vGWrLoxRO_IpW-SD2TdD5iMHXzsMzED-W4G_4BhJOeYpsKRb9g1yfSYSTOSixD8NscOhzR-KA5aEzKezPtx8fPy4vbsenHz42p9trpZ2IqLYeGmpaxy0krTNrQtlawBQDHRgEW0zlh0QiBFUzKBkkujjFSuoUBBqQqOi8977jbErOd3yZqJWvASgMGkWO8VLpqN3ibfmTTqaLz-dxDTvTZp8Dag5lK2tBEU-GQnq0a1ogImjAVeurrFifV1dts1HTqL_ZBMeAV9fdP7X_o-Puiyoqwq1QT4MgNS_L3DPPxn5HKvsinmnLB9dmBUPwbgqUs_BkDPAZjaPr2c7rnp6cfhL9AlsGA</recordid><startdate>20150714</startdate><enddate>20150714</enddate><creator>Smith, Rachel A S</creator><creator>Nabok, Aleksey</creator><creator>Blakeman, Ben J F</creator><creator>Xue, Wei-Feng</creator><creator>Abell, Benjamin</creator><creator>Smith, David P</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20150714</creationdate><title>Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry</title><author>Smith, Rachel A S ; Nabok, Aleksey ; Blakeman, Ben J F ; Xue, Wei-Feng ; Abell, Benjamin ; Smith, David P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-dddd8c8d7c7afb0f4879333816b3ceecdaced66e0ea416e727a8a78db03038853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>alpha-Synuclein - metabolism</topic><topic>alpha-Synuclein - toxicity</topic><topic>Alzheimer's disease</topic><topic>Alzheimers disease</topic><topic>Amyloid - metabolism</topic><topic>Amyloid - toxicity</topic><topic>Amyloid beta-Peptides - metabolism</topic><topic>Amyloid beta-Peptides - toxicity</topic><topic>Animals</topic><topic>Biocompatibility</topic><topic>Biological activity</topic><topic>Biomedical research</topic><topic>Biosensors</topic><topic>Cell Line, Tumor</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>Cell membranes</topic><topic>Cytotoxicity</topic><topic>Dye releases</topic><topic>E coli</topic><topic>Ellipsometry</topic><topic>Environmental monitoring</topic><topic>Fibrils</topic><topic>Humans</topic><topic>Lipids</topic><topic>Liposomes</topic><topic>Liposomes - metabolism</topic><topic>Membranes</topic><topic>Molecular structure</topic><topic>Muramidase - metabolism</topic><topic>Muramidase - toxicity</topic><topic>Mutation</topic><topic>Oligomers</topic><topic>Optical Phenomena</topic><topic>Peptide Fragments - 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Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce cytotoxicity. To investigate membrane disruption and cytotoxic effects associated with intact and fragmented fibrils, the novel in situ spectroscopic technique of Total Internal Reflection Ellipsometry (TIRE) was used. Fibril lipid interactions were monitored using natively derived whole cell membranes as a model of the in vivo environment. We show that fragmented fibrils have an increased ability to disrupt these natively derived membranes by causing a loss of material from the deposited surface when compared with unfragmented fibrils. This effect was corroborated by observations of membrane disruption in live cells, and by dye release assay using synthetic liposomes. Through these studies we demonstrate the use of TIRE for the analysis of protein-lipid interactions on natively derived lipid surfaces, and provide an explanation on how amyloid fibrils can cause a toxic gain of function, while entangled amyloid plaques exert minimal biological activity.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26172440</pmid><doi>10.1371/journal.pone.0132309</doi><oa>free_for_read</oa></addata></record> |
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| subjects | alpha-Synuclein - metabolism alpha-Synuclein - toxicity Alzheimer's disease Alzheimers disease Amyloid - metabolism Amyloid - toxicity Amyloid beta-Peptides - metabolism Amyloid beta-Peptides - toxicity Animals Biocompatibility Biological activity Biomedical research Biosensors Cell Line, Tumor Cell Membrane - drug effects Cell Membrane - metabolism Cell membranes Cytotoxicity Dye releases E coli Ellipsometry Environmental monitoring Fibrils Humans Lipids Liposomes Liposomes - metabolism Membranes Molecular structure Muramidase - metabolism Muramidase - toxicity Mutation Oligomers Optical Phenomena Peptide Fragments - metabolism Peptide Fragments - toxicity Peptides Protein Binding Proteins Senile plaques Studies Toxicity |
| title | Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry |
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