Non‐Adhesive Behavior of New Nanostructured PNIPAM Surfaces Towards Specific Neurodegenerative Proteins: Application to Storage and Titration of Tau Proteins
Identifieur interne : 001250 ( Main/Exploration ); précédent : 001249; suivant : 001251Non‐Adhesive Behavior of New Nanostructured PNIPAM Surfaces Towards Specific Neurodegenerative Proteins: Application to Storage and Titration of Tau Proteins
Auteurs : Tjasa Vrlinic [France] ; Dominique Debarnot [France] ; Gilbert Legeay [France] ; Arnaud Coudreuse [France] ; Benaissa El Moualij [Belgique] ; Willy Zorzi [Belgique] ; Armand Perret-Liaudet [France] ; Isabelle Quadrio [France] ; Miran Mozetic [Slovénie] ; Fabienne Poncin-Epaillard [France]Source :
- Macromolecular Bioscience [ 1616-5187 ] ; 2012-10.
English descriptors
- KwdEn :
Abstract
New nonfouling tubes are developed and their influence on the adhesion of neuroproteins is studied. The biomarkers are considered as single components (recombinant prion and Tau proteins) or in a solution of native and pathological forms. The samples are stored for 24 h at 4 °C in virgin and treated tubes layered with two different nanostructured coatings based on poly(N‐isopropylacrylamide) with either a positive or a neutral charge, and the protein adhesion is monitored. The recombinant protein with a high pI is repelled from the nanostructured surface that has a negative ζ potential, whereas the recombinant protein with the lower pI is attracted. Furthermore, in the case of complex solutions, neutral nanostructured surfaces are able to retain all amyloid biomarkers.
Url:
DOI: 10.1002/mabi.201200116
Affiliations:
- Belgique, France, Slovénie
- Auvergne-Rhône-Alpes, Pays de la Loire, Province de Liège, Rhône-Alpes, Région wallonne
- Bron, Le Mans, Liège
- Université de Liège
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Biosci.</title><idno type="ISSN">1616-5187</idno><idno type="eISSN">1616-5195</idno><imprint><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2012-10">2012-10</date><biblScope unit="volume">12</biblScope><biblScope unit="issue">10</biblScope><biblScope unit="page" from="1354">1354</biblScope><biblScope unit="page" to="1363">1363</biblScope></imprint><idno type="ISSN">1616-5187</idno></series><idno type="istex">90D5058838FF5E295B1FFDE9750FC21C2A2AE778</idno><idno type="DOI">10.1002/mabi.201200116</idno><idno type="ArticleID">MABI201200116</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1616-5187</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ELISA</term><term>biomolecules</term><term>nanostructuring</term><term>non‐adhesion</term><term>plasma treatment</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">New nonfouling tubes are developed and their influence on the adhesion of neuroproteins is studied. The biomarkers are considered as single components (recombinant prion and Tau proteins) or in a solution of native and pathological forms. The samples are stored for 24 h at 4 °C in virgin and treated tubes layered with two different nanostructured coatings based on poly(N‐isopropylacrylamide) with either a positive or a neutral charge, and the protein adhesion is monitored. The recombinant protein with a high pI is repelled from the nanostructured surface that has a negative ζ potential, whereas the recombinant protein with the lower pI is attracted. Furthermore, in the case of complex solutions, neutral nanostructured surfaces are able to retain all amyloid biomarkers.</div></front></TEI><affiliations><list><country><li>Belgique</li><li>France</li><li>Slovénie</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Pays de la Loire</li><li>Province de Liège</li><li>Rhône-Alpes</li><li>Région wallonne</li></region><settlement><li>Bron</li><li>Le Mans</li><li>Liège</li></settlement><orgName><li>Université de Liège</li></orgName></list><tree><country name="France"><region name="Pays de la Loire"><name sortKey="Vrlinic, Tjasa" sort="Vrlinic, Tjasa" uniqKey="Vrlinic T" first="Tjasa" last="Vrlinic">Tjasa Vrlinic</name></region><name sortKey="Coudreuse, Arnaud" sort="Coudreuse, Arnaud" uniqKey="Coudreuse A" first="Arnaud" last="Coudreuse">Arnaud Coudreuse</name><name sortKey="Debarnot, Dominique" sort="Debarnot, Dominique" uniqKey="Debarnot D" first="Dominique" last="Debarnot">Dominique Debarnot</name><name sortKey="Legeay, Gilbert" sort="Legeay, Gilbert" uniqKey="Legeay G" first="Gilbert" last="Legeay">Gilbert Legeay</name><name sortKey="Perret Iaudet, Armand" sort="Perret Iaudet, Armand" uniqKey="Perret Iaudet A" first="Armand" last="Perret-Liaudet">Armand Perret-Liaudet</name><name sortKey="Poncin Paillard, Fabienne" sort="Poncin Paillard, Fabienne" uniqKey="Poncin Paillard F" first="Fabienne" last="Poncin-Epaillard">Fabienne Poncin-Epaillard</name><name sortKey="Poncin Paillard, Fabienne" sort="Poncin Paillard, Fabienne" uniqKey="Poncin Paillard F" first="Fabienne" last="Poncin-Epaillard">Fabienne Poncin-Epaillard</name><name sortKey="Quadrio, Isabelle" sort="Quadrio, Isabelle" uniqKey="Quadrio I" first="Isabelle" last="Quadrio">Isabelle Quadrio</name></country><country name="Belgique"><region name="Région wallonne"><name sortKey="El Moualij, Benaissa" sort="El Moualij, Benaissa" uniqKey="El Moualij B" first="Benaissa" last="El Moualij">Benaissa El Moualij</name></region><name sortKey="Zorzi, Willy" sort="Zorzi, Willy" uniqKey="Zorzi W" first="Willy" last="Zorzi">Willy Zorzi</name></country><country name="Slovénie"><noRegion><name sortKey="Mozetic, Miran" sort="Mozetic, Miran" uniqKey="Mozetic M" first="Miran" last="Mozetic">Miran Mozetic</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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