Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different
Amyloid polymorphism of twisted and straight β-endorphin fibrils was studied by negative-stain transmission electron microscopy, scanning transmission electron microscopy, and solid-state nuclear magnetic resonance spectroscopy. Whereas fibrils assembled in the presence of salt formed flat, striated...
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| Veröffentlicht in: | The journal of physical chemistry. B 2017-03, Vol.121 (8), p.1783-1792 |
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| container_title | The journal of physical chemistry. B |
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| creator | Seuring, Carolin Verasdonck, Joeri Ringler, Philippe Cadalbert, Riccardo Stahlberg, Henning Böckmann, Anja Meier, Beat H Riek, Roland |
| description | Amyloid polymorphism of twisted and straight β-endorphin fibrils was studied by negative-stain transmission electron microscopy, scanning transmission electron microscopy, and solid-state nuclear magnetic resonance spectroscopy. Whereas fibrils assembled in the presence of salt formed flat, striated ribbons, in the absence of salt they formed mainly twisted filaments. To get insights into their structural differences at the atomic level, 3D solid-state NMR spectra of both fibril types were acquired, allowing the detection of the differences in chemical shifts of 13C and 15N atoms in both preparations. The spectral fingerprints and therefore the chemical shifts are very similar for both fibril types. This indicates that the monomer structure and the molecular interfaces are almost the same but that these small differences do propagate to produce flat and twisted morphologies at the mesoscopic scale. This finding is in agreement with both experimental and theoretical considerations on the assembly of polymers (including amyloids) under different salt conditions, which attribute the mesoscopic difference of flat versus twisted fibrils to electrostatic intermolecular repulsions. |
| doi_str_mv | 10.1021/acs.jpcb.6b10624 |
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Whereas fibrils assembled in the presence of salt formed flat, striated ribbons, in the absence of salt they formed mainly twisted filaments. To get insights into their structural differences at the atomic level, 3D solid-state NMR spectra of both fibril types were acquired, allowing the detection of the differences in chemical shifts of 13C and 15N atoms in both preparations. The spectral fingerprints and therefore the chemical shifts are very similar for both fibril types. This indicates that the monomer structure and the molecular interfaces are almost the same but that these small differences do propagate to produce flat and twisted morphologies at the mesoscopic scale. This finding is in agreement with both experimental and theoretical considerations on the assembly of polymers (including amyloids) under different salt conditions, which attribute the mesoscopic difference of flat versus twisted fibrils to electrostatic intermolecular repulsions.</description><identifier>ISSN: 1520-6106</identifier><identifier>EISSN: 1520-5207</identifier><identifier>DOI: 10.1021/acs.jpcb.6b10624</identifier><identifier>PMID: 28075583</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amyloid - chemistry ; Amyloid - ultrastructure ; Analytical chemistry ; Atomic structure ; beta-Endorphin - chemistry ; Chemical Sciences ; Fingerprints ; Flats (landforms) ; Humans ; Microscopy, Electron, Scanning Transmission ; Molecular structure ; Nuclear magnetic resonance ; Nuclear Magnetic Resonance, Biomolecular ; Polymorphism ; Protein Multimerization ; Protein Structure, Secondary ; Ribbons ; Sodium Chloride - chemistry ; Spectra</subject><ispartof>The journal of physical chemistry. 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B</title><addtitle>J. Phys. Chem. B</addtitle><description>Amyloid polymorphism of twisted and straight β-endorphin fibrils was studied by negative-stain transmission electron microscopy, scanning transmission electron microscopy, and solid-state nuclear magnetic resonance spectroscopy. Whereas fibrils assembled in the presence of salt formed flat, striated ribbons, in the absence of salt they formed mainly twisted filaments. To get insights into their structural differences at the atomic level, 3D solid-state NMR spectra of both fibril types were acquired, allowing the detection of the differences in chemical shifts of 13C and 15N atoms in both preparations. The spectral fingerprints and therefore the chemical shifts are very similar for both fibril types. This indicates that the monomer structure and the molecular interfaces are almost the same but that these small differences do propagate to produce flat and twisted morphologies at the mesoscopic scale. This finding is in agreement with both experimental and theoretical considerations on the assembly of polymers (including amyloids) under different salt conditions, which attribute the mesoscopic difference of flat versus twisted fibrils to electrostatic intermolecular repulsions.</description><subject>Amyloid - chemistry</subject><subject>Amyloid - ultrastructure</subject><subject>Analytical chemistry</subject><subject>Atomic structure</subject><subject>beta-Endorphin - chemistry</subject><subject>Chemical Sciences</subject><subject>Fingerprints</subject><subject>Flats (landforms)</subject><subject>Humans</subject><subject>Microscopy, Electron, Scanning Transmission</subject><subject>Molecular structure</subject><subject>Nuclear magnetic resonance</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Polymorphism</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Secondary</subject><subject>Ribbons</subject><subject>Sodium Chloride - chemistry</subject><subject>Spectra</subject><issn>1520-6106</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUFv1DAQhS0EoqXlzgn5CFJ38cRx4nCLSksrLYJD4Woce6J15ayDna2Uf1-HXXpDqqWRrfH3nsZ-hLwDtgZWwCdt0vp-NN266oBVRfmCnIIo2CpX_fJ4rvLNCXmT0j1jhShk9ZqcFJLVQkh-Sn63w-yDs_TaddF5-iP4eQhx3Lo0fKatH0Ka6K3F3eSM9jTs6LRF2k5hcIZu8AH9Bf2GKSQTxoXwM_2FcaZfXN9jzLJz8qrXPuHb435Gfl5f3V3erDbfv95etpuVFqyY8pS6F0ZYYZsKRNOg1n0HkN8kS-xEBQZtxTvLoUJeamgs60QvpLSlhbz4Gfl48N1qr8boBh1nFbRTN-1GLT3GeVkLJh4W9sOBHWP4s8c0qcElg97rHYZ9UiAbLmUNBX8GKqEuG1aXz0CFBGANiIyyA2piSCli_zQxMLUkq3KyaklWHZPNkvdH9303oH0S_IsyAxcH4K807OMuf_f__R4BiMetVA</recordid><startdate>20170302</startdate><enddate>20170302</enddate><creator>Seuring, Carolin</creator><creator>Verasdonck, Joeri</creator><creator>Ringler, Philippe</creator><creator>Cadalbert, Riccardo</creator><creator>Stahlberg, Henning</creator><creator>Böckmann, Anja</creator><creator>Meier, Beat H</creator><creator>Riek, Roland</creator><general>American Chemical Society</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>7X8</scope><scope>7TK</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-6333-066X</orcidid><orcidid>https://orcid.org/0000-0002-1185-4592</orcidid><orcidid>https://orcid.org/0000-0002-9107-4464</orcidid><orcidid>https://orcid.org/0000-0001-8149-7941</orcidid></search><sort><creationdate>20170302</creationdate><title>Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different</title><author>Seuring, Carolin ; 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| subjects | Amyloid - chemistry Amyloid - ultrastructure Analytical chemistry Atomic structure beta-Endorphin - chemistry Chemical Sciences Fingerprints Flats (landforms) Humans Microscopy, Electron, Scanning Transmission Molecular structure Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Polymorphism Protein Multimerization Protein Structure, Secondary Ribbons Sodium Chloride - chemistry Spectra |
| title | Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different |
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