An efficient procedure for removal and inactivation of alpha-synuclein assemblies from laboratory materials.
Identifieur interne : 000076 ( Hal/Corpus ); précédent : 000075; suivant : 000077An efficient procedure for removal and inactivation of alpha-synuclein assemblies from laboratory materials.
Auteurs : Luc Bousset ; Patrik Brundin ; Anja Böckmann ; Beat Meier ; Ronald MelkiSource :
- Journal of Parkinson's disease [ 1877-718X ] ; 2016-01-04.
Abstract
Preformed α-synuclein fibrils seed the aggregation of soluble α-synuclein in cultured cells and in vivo. This, and other findings, has kindled the idea that α-synuclein fibrils possess prion-like properties. As α-synuclein fibrils should not be considered as innocuous, there is a need for decontamination and inactivation procedures for laboratory benches and non-disposable laboratory material. We assessed the effectiveness of different procedures designed to disassemble α-synuclein fibrils and reduce their infectivity. We examined different commercially available detergents to remove α-synuclein assemblies adsorbed on materials that are not disposable and that are most found in laboratories (e.g. plastic, glass, aluminum or stainless steel surfaces). We show that methods designed to decrease PrP prion infectivity neither effectively remove α-synuclein assemblies adsorbed to different materials commonly used in the laboratory nor disassemble the fibrillar form of the protein with efficiency. In contrast, both commercial detergents and SDS detached α-synuclein assemblies from contaminated surfaces and disassembled the fibrils. We describe three cleaning procedures that effectively remove and disassemble α-synuclein seeds. The methods rely on the use of detergents that are compatible with most non-disposable tools in a laboratory. The procedures are easy to implement and significantly decrease any potential risks associated to handling α-synuclein assemblies.
Url:
DOI: 10.3233/JPD-150691
Links to Exploration step
Hal:hal-01240203Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">An efficient procedure for removal and inactivation of alpha-synuclein assemblies from laboratory materials.</title>
<author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-418266" status="VALID"> <orgName>Institut des Neurosciences de Paris-Saclay</orgName>
<orgName type="acronym">Neuro-PSI</orgName>
<desc> <address> <addrLine>Centre National de la Recherche Scientifique, Unité Mixte de Recherche-9197 Université Paris-Sudbâtiment 32 Campus de Recherche de Gif-sur-Yvette1, avenue de la Terrasse91198 Gif-sur-Yvette</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://neuro-psi.fr</ref>
</desc>
<listRelation> <relation active="#struct-92966" type="direct"></relation>
<relation name="UMR9197" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-92966" type="direct"><org type="institution" xml:id="struct-92966" status="VALID"> <orgName>Université Paris-Sud - Paris 11</orgName>
<orgName type="acronym">UP11</orgName>
<desc> <address> <addrLine>Bâtiment 300 - 91405 Orsay cedex</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.u-psud.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="UMR9197" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
</affiliation>
</author>
<author><name sortKey="Brundin, Patrik" sort="Brundin, Patrik" uniqKey="Brundin P" first="Patrik" last="Brundin">Patrik Brundin</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-164471" status="INCOMING"> <orgName>Van Andel Research Institute, Grand Rapids, Michigan</orgName>
<desc> <address> <country key="US"></country>
</address>
</desc>
<listRelation> <relation active="#struct-341695" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-341695" type="direct"><org type="institution" xml:id="struct-341695" status="INCOMING"> <orgName>Van Andel Research Institute, Grand Rapids, Michigan</orgName>
<desc> <address> <country key="FR"></country>
</address>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
</affiliation>
</author>
<author><name sortKey="Bockmann, Anja" sort="Bockmann, Anja" uniqKey="Bockmann A" first="Anja" last="Böckmann">Anja Böckmann</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-227725" status="VALID"> <orgName>Institut de biologie et chimie des protéines [Lyon]</orgName>
<orgName type="acronym">IBCP</orgName>
<desc> <address> <addrLine>7 Passage du Vercors 69367 LYON CEDEX 07</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.ibcp.fr</ref>
</desc>
<listRelation> <relation active="#struct-194495" type="direct"></relation>
<relation name="FR3302" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-194495" type="direct"><org type="institution" xml:id="struct-194495" status="VALID"><orgName>Université Claude Bernard Lyon 1</orgName>
<orgName type="acronym">UCBL</orgName>
<desc><address><addrLine>43, boulevard du 11 novembre 1918, 69622 Villeurbanne cedex</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.univ-lyon1.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="FR3302" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
</affiliation>
</author>
<author><name sortKey="Meier, Beat" sort="Meier, Beat" uniqKey="Meier B" first="Beat" last="Meier">Beat Meier</name>
<affiliation><hal:affiliation type="institution" xml:id="struct-425064" status="INCOMING"> <orgName>Physical Chemistry, ETH Zürich</orgName>
<desc> <address> <addrLine>Wolfgang-Pauli-Strasse 10, 8093, Zurich</addrLine>
<country key="CH"></country>
</address>
</desc>
</hal:affiliation>
</affiliation>
</author>
<author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-418266" status="VALID"> <orgName>Institut des Neurosciences de Paris-Saclay</orgName>
<orgName type="acronym">Neuro-PSI</orgName>
<desc> <address> <addrLine>Centre National de la Recherche Scientifique, Unité Mixte de Recherche-9197 Université Paris-Sudbâtiment 32 Campus de Recherche de Gif-sur-Yvette1, avenue de la Terrasse91198 Gif-sur-Yvette</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://neuro-psi.fr</ref>
</desc>
<listRelation> <relation active="#struct-92966" type="direct"></relation>
<relation name="UMR9197" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-92966" type="direct"><org type="institution" xml:id="struct-92966" status="VALID"> <orgName>Université Paris-Sud - Paris 11</orgName>
<orgName type="acronym">UP11</orgName>
<desc> <address> <addrLine>Bâtiment 300 - 91405 Orsay cedex</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.u-psud.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="UMR9197" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">HAL</idno>
<idno type="RBID">Hal:hal-01240203</idno>
<idno type="halId">hal-01240203</idno>
<idno type="halUri">https://hal.archives-ouvertes.fr/hal-01240203</idno>
<idno type="url">https://hal.archives-ouvertes.fr/hal-01240203</idno>
<idno type="doi">10.3233/JPD-150691</idno>
<date when="2016-01-04">2016-01-04</date>
<idno type="wicri:Area/Hal/Corpus">000076</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">An efficient procedure for removal and inactivation of alpha-synuclein assemblies from laboratory materials.</title>
<author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-418266" status="VALID"> <orgName>Institut des Neurosciences de Paris-Saclay</orgName>
<orgName type="acronym">Neuro-PSI</orgName>
<desc> <address> <addrLine>Centre National de la Recherche Scientifique, Unité Mixte de Recherche-9197 Université Paris-Sudbâtiment 32 Campus de Recherche de Gif-sur-Yvette1, avenue de la Terrasse91198 Gif-sur-Yvette</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://neuro-psi.fr</ref>
</desc>
<listRelation> <relation active="#struct-92966" type="direct"></relation>
<relation name="UMR9197" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-92966" type="direct"><org type="institution" xml:id="struct-92966" status="VALID"> <orgName>Université Paris-Sud - Paris 11</orgName>
<orgName type="acronym">UP11</orgName>
<desc> <address> <addrLine>Bâtiment 300 - 91405 Orsay cedex</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.u-psud.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="UMR9197" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
</affiliation>
</author>
<author><name sortKey="Brundin, Patrik" sort="Brundin, Patrik" uniqKey="Brundin P" first="Patrik" last="Brundin">Patrik Brundin</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-164471" status="INCOMING"> <orgName>Van Andel Research Institute, Grand Rapids, Michigan</orgName>
<desc> <address> <country key="US"></country>
</address>
</desc>
<listRelation> <relation active="#struct-341695" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-341695" type="direct"><org type="institution" xml:id="struct-341695" status="INCOMING"> <orgName>Van Andel Research Institute, Grand Rapids, Michigan</orgName>
<desc> <address> <country key="FR"></country>
</address>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
</affiliation>
</author>
<author><name sortKey="Bockmann, Anja" sort="Bockmann, Anja" uniqKey="Bockmann A" first="Anja" last="Böckmann">Anja Böckmann</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-227725" status="VALID"> <orgName>Institut de biologie et chimie des protéines [Lyon]</orgName>
<orgName type="acronym">IBCP</orgName>
<desc> <address> <addrLine>7 Passage du Vercors 69367 LYON CEDEX 07</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.ibcp.fr</ref>
</desc>
<listRelation> <relation active="#struct-194495" type="direct"></relation>
<relation name="FR3302" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-194495" type="direct"><org type="institution" xml:id="struct-194495" status="VALID"><orgName>Université Claude Bernard Lyon 1</orgName>
<orgName type="acronym">UCBL</orgName>
<desc><address><addrLine>43, boulevard du 11 novembre 1918, 69622 Villeurbanne cedex</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.univ-lyon1.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="FR3302" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
</affiliation>
</author>
<author><name sortKey="Meier, Beat" sort="Meier, Beat" uniqKey="Meier B" first="Beat" last="Meier">Beat Meier</name>
<affiliation><hal:affiliation type="institution" xml:id="struct-425064" status="INCOMING"> <orgName>Physical Chemistry, ETH Zürich</orgName>
<desc> <address> <addrLine>Wolfgang-Pauli-Strasse 10, 8093, Zurich</addrLine>
<country key="CH"></country>
</address>
</desc>
</hal:affiliation>
</affiliation>
</author>
<author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name>
<affiliation><hal:affiliation type="laboratory" xml:id="struct-418266" status="VALID"> <orgName>Institut des Neurosciences de Paris-Saclay</orgName>
<orgName type="acronym">Neuro-PSI</orgName>
<desc> <address> <addrLine>Centre National de la Recherche Scientifique, Unité Mixte de Recherche-9197 Université Paris-Sudbâtiment 32 Campus de Recherche de Gif-sur-Yvette1, avenue de la Terrasse91198 Gif-sur-Yvette</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://neuro-psi.fr</ref>
</desc>
<listRelation> <relation active="#struct-92966" type="direct"></relation>
<relation name="UMR9197" active="#struct-441569" type="direct"></relation>
</listRelation>
<tutelles><tutelle active="#struct-92966" type="direct"><org type="institution" xml:id="struct-92966" status="VALID"> <orgName>Université Paris-Sud - Paris 11</orgName>
<orgName type="acronym">UP11</orgName>
<desc> <address> <addrLine>Bâtiment 300 - 91405 Orsay cedex</addrLine>
<country key="FR"></country>
</address>
<ref type="url">http://www.u-psud.fr/</ref>
</desc>
</org>
</tutelle>
<tutelle name="UMR9197" active="#struct-441569" type="direct"><org type="institution" xml:id="struct-441569" status="VALID"> <idno type="IdRef">02636817X</idno>
<idno type="ISNI">0000000122597504</idno>
<orgName>Centre National de la Recherche Scientifique</orgName>
<orgName type="acronym">CNRS</orgName>
<date type="start">1939-10-19</date>
<desc> <address> <country key="FR"></country>
</address>
<ref type="url">http://www.cnrs.fr/</ref>
</desc>
</org>
</tutelle>
</tutelles>
</hal:affiliation>
</affiliation>
</author>
</analytic>
<idno type="DOI">10.3233/JPD-150691</idno>
<series><title level="j">Journal of Parkinson's disease</title>
<idno type="ISSN">1877-718X</idno>
<imprint><date type="datePub">2016-01-04</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Preformed α-synuclein fibrils seed the aggregation of soluble α-synuclein in cultured cells and in vivo. This, and other findings, has kindled the idea that α-synuclein fibrils possess prion-like properties. As α-synuclein fibrils should not be considered as innocuous, there is a need for decontamination and inactivation procedures for laboratory benches and non-disposable laboratory material. We assessed the effectiveness of different procedures designed to disassemble α-synuclein fibrils and reduce their infectivity. We examined different commercially available detergents to remove α-synuclein assemblies adsorbed on materials that are not disposable and that are most found in laboratories (e.g. plastic, glass, aluminum or stainless steel surfaces). We show that methods designed to decrease PrP prion infectivity neither effectively remove α-synuclein assemblies adsorbed to different materials commonly used in the laboratory nor disassemble the fibrillar form of the protein with efficiency. In contrast, both commercial detergents and SDS detached α-synuclein assemblies from contaminated surfaces and disassembled the fibrils. We describe three cleaning procedures that effectively remove and disassemble α-synuclein seeds. The methods rely on the use of detergents that are compatible with most non-disposable tools in a laboratory. The procedures are easy to implement and significantly decrease any potential risks associated to handling α-synuclein assemblies. </div>
</front>
</TEI>
<hal api="V3"> <titleStmt> <title xml:lang="en">An efficient procedure for removal and inactivation of alpha-synuclein assemblies from laboratory materials.</title>
<author role="aut"> <persName> <forename type="first">Luc</forename>
<surname>Bousset</surname>
</persName>
<idno type="halauthorid">190085</idno>
<affiliation ref="#struct-418266"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Patrik</forename>
<surname>Brundin</surname>
</persName>
<idno type="halauthorid">1193639</idno>
<affiliation ref="#struct-164471"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Anja</forename>
<surname>Böckmann</surname>
</persName>
<idno type="halauthorid">104714</idno>
<affiliation ref="#struct-227725"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Beat</forename>
<surname>Meier</surname>
</persName>
<idno type="halauthorid">1257911</idno>
<affiliation ref="#struct-425064"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Ronald</forename>
<surname>Melki</surname>
</persName>
<idno type="halauthorid">190086</idno>
<affiliation ref="#struct-418266"></affiliation>
</author>
<editor role="depositor"> <persName> <forename>Alain</forename>
<surname>PERIGNON</surname>
</persName>
<email type="md5">0915a8bc0b5a494fc86eb9724296445c</email>
<email type="domain">cnrs.fr</email>
</editor>
</titleStmt>
<editionStmt> <edition n="v1" type="current"> <date type="whenSubmitted">2015-12-08 18:01:33</date>
<date type="whenModified">2017-02-09 16:08:23</date>
<date type="whenReleased">2015-12-08 18:01:33</date>
<date type="whenProduced">2016-01-04</date>
</edition>
<respStmt> <resp>contributor</resp>
<name key="108746"> <persName> <forename>Alain</forename>
<surname>PERIGNON</surname>
</persName>
<email type="md5">0915a8bc0b5a494fc86eb9724296445c</email>
<email type="domain">cnrs.fr</email>
</name>
</respStmt>
</editionStmt>
<publicationStmt> <distributor>CCSD</distributor>
<idno type="halId">hal-01240203</idno>
<idno type="halUri">https://hal.archives-ouvertes.fr/hal-01240203</idno>
<idno type="halBibtex">bousset:hal-01240203</idno>
<idno type="halRefHtml">Journal of Parkinson's disease, Amsterdam : b : IOS Press, 2016, 6 (1), pp.143-51. <10.3233/JPD-150691></idno>
<idno type="halRef">Journal of Parkinson's disease, Amsterdam : b : IOS Press, 2016, 6 (1), pp.143-51. <10.3233/JPD-150691></idno>
</publicationStmt>
<seriesStmt> <idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno>
<idno type="stamp" n="INRIA-CHILE">INRIA Chile</idno>
<idno type="stamp" n="UNIV-PSUD-SACLAY" p="UNIV-PARIS-SACLAY">Université Paris Sud pour Paris Saclay</idno>
</seriesStmt>
<notesStmt> <note type="audience" n="2">International</note>
<note type="popular" n="0">No</note>
<note type="peer" n="1">Yes</note>
</notesStmt>
<sourceDesc> <biblStruct> <analytic> <title xml:lang="en">An efficient procedure for removal and inactivation of alpha-synuclein assemblies from laboratory materials.</title>
<author role="aut"> <persName> <forename type="first">Luc</forename>
<surname>Bousset</surname>
</persName>
<idno type="halauthorid">190085</idno>
<affiliation ref="#struct-418266"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Patrik</forename>
<surname>Brundin</surname>
</persName>
<idno type="halauthorid">1193639</idno>
<affiliation ref="#struct-164471"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Anja</forename>
<surname>Böckmann</surname>
</persName>
<idno type="halauthorid">104714</idno>
<affiliation ref="#struct-227725"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Beat</forename>
<surname>Meier</surname>
</persName>
<idno type="halauthorid">1257911</idno>
<affiliation ref="#struct-425064"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Ronald</forename>
<surname>Melki</surname>
</persName>
<idno type="halauthorid">190086</idno>
<affiliation ref="#struct-418266"></affiliation>
</author>
</analytic>
<monogr> <idno type="halJournalId" status="VALID">103225</idno>
<idno type="issn">1877-718X</idno>
<idno type="eissn">1877-7171</idno>
<title level="j">Journal of Parkinson's disease</title>
<imprint> <publisher>Amsterdam : b : IOS Press</publisher>
<biblScope unit="volume">6</biblScope>
<biblScope unit="issue">1</biblScope>
<biblScope unit="pp">143-51</biblScope>
<date type="datePub">2016-01-04</date>
</imprint>
</monogr>
<idno type="pubmed">26639448</idno>
<idno type="doi">10.3233/JPD-150691</idno>
</biblStruct>
</sourceDesc>
<profileDesc> <langUsage> <language ident="en">English</language>
</langUsage>
<textClass> <classCode scheme="halDomain" n="sdv.neu.nb">Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology</classCode>
<classCode scheme="halDomain" n="sdv.neu.pc">Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Psychology and behavior</classCode>
<classCode scheme="halDomain" n="sdv.neu.sc">Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Cognitive Sciences</classCode>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
</textClass>
<abstract xml:lang="en">Preformed α-synuclein fibrils seed the aggregation of soluble α-synuclein in cultured cells and in vivo. This, and other findings, has kindled the idea that α-synuclein fibrils possess prion-like properties. As α-synuclein fibrils should not be considered as innocuous, there is a need for decontamination and inactivation procedures for laboratory benches and non-disposable laboratory material. We assessed the effectiveness of different procedures designed to disassemble α-synuclein fibrils and reduce their infectivity. We examined different commercially available detergents to remove α-synuclein assemblies adsorbed on materials that are not disposable and that are most found in laboratories (e.g. plastic, glass, aluminum or stainless steel surfaces). We show that methods designed to decrease PrP prion infectivity neither effectively remove α-synuclein assemblies adsorbed to different materials commonly used in the laboratory nor disassemble the fibrillar form of the protein with efficiency. In contrast, both commercial detergents and SDS detached α-synuclein assemblies from contaminated surfaces and disassembled the fibrils. We describe three cleaning procedures that effectively remove and disassemble α-synuclein seeds. The methods rely on the use of detergents that are compatible with most non-disposable tools in a laboratory. The procedures are easy to implement and significantly decrease any potential risks associated to handling α-synuclein assemblies. </abstract>
</profileDesc>
</hal>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/Hal/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000076 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Hal/Corpus/biblio.hfd -nk 000076 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= ParkinsonFranceV1 |flux= Hal |étape= Corpus |type= RBID |clé= Hal:hal-01240203 |texte= An efficient procedure for removal and inactivation of alpha-synuclein assemblies from laboratory materials. }}
![]() | This area was generated with Dilib version V0.6.29. | ![]() |