Nanomechanical properties of distinct fibrillar polymorphs of the protein α-synuclein
Identifieur interne : 000225 ( Main/Exploration ); précédent : 000224; suivant : 000226Nanomechanical properties of distinct fibrillar polymorphs of the protein α-synuclein
Auteurs : Ali Makky [France] ; Luc Bousset [France] ; Jérôme Polesel-Maris [Luxembourg (pays)] ; Ronald Melki [France]Source :
- Scientific Reports [ 2045-2322 ] ; 2016.
Abstract
Alpha-synuclein (α-Syn) is a small presynaptic protein of 140 amino acids. Its pathologic intracellular aggregation within the central nervous system yields protein fibrillar inclusions named Lewy bodies that are the hallmarks of Parkinson’s disease (PD). In solution, pure α-Syn adopts an intrinsically disordered structure and assembles into fibrils that exhibit considerable morphological heterogeneity depending on their assembly conditions. We recently established tightly controlled experimental conditions allowing the assembly of α-Syn into highly homogeneous and pure polymorphs. The latter exhibited differences in their shape, their structure but also in their functional properties. We have conducted an AFM study at high resolution and performed a statistical analysis of fibrillar α-Syn shape and thermal fluctuations to calculate the persistence length to further assess the nanomechanical properties of α-Syn polymorphs. Herein, we demonstrated quantitatively that distinct polymorphs made of the same protein (wild-type α-Syn) show significant differences in their morphology (height, width and periodicity) and physical properties (persistence length, bending rigidity and axial Young’s modulus).
Url:
DOI: 10.1038/srep37970
PubMed: 27901068
PubMed Central: 5128817
Affiliations:
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Paris-Sud, University Paris-Saclay</institution>, 92296 Châtenay-Malabry,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name><affiliation wicri:level="1"><nlm:aff id="a2"><institution>Paris-Saclay Institute of Neuroscience, Centre National de la Recherche Scientifique, Université Paris-Saclay</institution>, 91190 Gif-sur-Yvette,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Polesel Maris, Jerome" sort="Polesel Maris, Jerome" uniqKey="Polesel Maris J" first="Jérôme" last="Polesel-Maris">Jérôme Polesel-Maris</name><affiliation wicri:level="1"><nlm:aff id="a3"><institution>Luxembourg Institute of Science and Technology (LIST), Materials Research and Technology (MRT)</institution>, L-4422 Belvaux,<country>Luxembourg</country></nlm:aff><country xml:lang="fr">Luxembourg (pays)</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><affiliation wicri:level="1"><nlm:aff id="a2"><institution>Paris-Saclay Institute of Neuroscience, Centre National de la Recherche Scientifique, Université Paris-Saclay</institution>, 91190 Gif-sur-Yvette,<country>France</country></nlm:aff><country xml:lang="fr">France</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Scientific Reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Alpha-synuclein (α-Syn) is a small presynaptic protein of 140 amino acids. Its pathologic intracellular aggregation within the central nervous system yields protein fibrillar inclusions named Lewy bodies that are the hallmarks of Parkinson’s disease (PD). In solution, pure α-Syn adopts an intrinsically disordered structure and assembles into fibrils that exhibit considerable morphological heterogeneity depending on their assembly conditions. We recently established tightly controlled experimental conditions allowing the assembly of α-Syn into highly homogeneous and pure polymorphs. The latter exhibited differences in their shape, their structure but also in their functional properties. We have conducted an AFM study at high resolution and performed a statistical analysis of fibrillar α-Syn shape and thermal fluctuations to calculate the persistence length to further assess the nanomechanical properties of α-Syn polymorphs. Herein, we demonstrated quantitatively that distinct polymorphs made of the same protein (wild-type α-Syn) show significant differences in their morphology (height, width and periodicity) and physical properties (persistence length, bending rigidity and axial Young’s modulus).</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Bousset, L" uniqKey="Bousset L">L. Bousset</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Spillantini, M G" uniqKey="Spillantini M">M. G. Spillantini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Spillantini, M G" uniqKey="Spillantini M">M. G. Spillantini</name></author><author><name sortKey="Crowther, R A" uniqKey="Crowther R">R. A. Crowther</name></author><author><name sortKey="Jakes, R" uniqKey="Jakes R">R. Jakes</name></author><author><name sortKey="Hasegawa, M" uniqKey="Hasegawa M">M. 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Knowles</name></author><author><name sortKey="Dobson, C M" uniqKey="Dobson C">C. M. Dobson</name></author><author><name sortKey="Macphee, C E" uniqKey="Macphee C">C. E. Macphee</name></author><author><name sortKey="Welland, M E" uniqKey="Welland M">M. E. Welland</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Vandenakker, C C" uniqKey="Vandenakker C">C. C. vandenAkker</name></author><author><name sortKey="Engel, M F M" uniqKey="Engel M">M. F. M. Engel</name></author><author><name sortKey="Velikov, K P" uniqKey="Velikov K">K. P. Velikov</name></author><author><name sortKey="Bonn, M" uniqKey="Bonn M">M. Bonn</name></author><author><name sortKey="Koenderink, G H" uniqKey="Koenderink G">G. H. Koenderink</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ghee, M" uniqKey="Ghee M">M. Ghee</name></author><author><name sortKey="Melki, R" uniqKey="Melki R">R. 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Verasdonck</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>France</li><li>Luxembourg (pays)</li></country></list><tree><country name="France"><noRegion><name sortKey="Makky, Ali" sort="Makky, Ali" uniqKey="Makky A" first="Ali" last="Makky">Ali Makky</name></noRegion><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name></country><country name="Luxembourg (pays)"><noRegion><name sortKey="Polesel Maris, Jerome" sort="Polesel Maris, Jerome" uniqKey="Polesel Maris J" first="Jérôme" last="Polesel-Maris">Jérôme Polesel-Maris</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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