Biomimetic Organization: Octapeptide Self-Assembly into Nanotubes of Viral Capsid-like Dimension
The controlled self-assembly of complex molecules into well defined hierarchical structures is a promising route for fabricating nanostructures. These nanoscale structures can be realized by naturally occurring proteins such as tobacco mosaic virus, capsid proteins, tubulin, actin, etc. Here, we rep...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2003-09, Vol.100 (18), p.10258-10262 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 10262 |
|---|---|
| container_issue | 18 |
| container_start_page | 10258 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 100 |
| creator | Valéry, Céline Paternostre, Maïté Robert, Bruno Gulik-Krzywicki, Thaddée Narayanan, Theyencheri Dedieu, Jean-Claude Keller, Gérard Torres, Maria-Luisa Cherif-Cheikh, Roland Calvo, Pilar Artzner, Franck |
| description | The controlled self-assembly of complex molecules into well defined hierarchical structures is a promising route for fabricating nanostructures. These nanoscale structures can be realized by naturally occurring proteins such as tobacco mosaic virus, capsid proteins, tubulin, actin, etc. Here, we report a simple alternative method based on self-assembling nanotubes formed by a synthetic therapeutic octapeptide, Lanreotide in water. We used a multidisciplinary approach involving optical and electron microscopies, vibrational spectroscopies, and small and wide angle x-ray scattering to elucidate the hierarchy of structures exhibited by this system. The results revealed the hexagonal packing of nanotubes, and high degree of monodispersity in the tube diameter (244 Å) and wall thickness (≈18 Å). Moreover, the diameter is tunable by suitable modifications in the molecular structure. The self-assembly of the nanotubes occurs through the association of β-sheets driven by amphiphilicity and a systematic aromatic/aliphatic side chain segregation. This original and simple system is a unique example for the study of complex self-assembling processes generated by de novo molecules or amyloid peptides. |
| doi_str_mv | 10.1073/pnas.1730609100 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_proqu</sourceid><recordid>TN_cdi_proquest_journals_201352776</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3147703</jstor_id><sourcerecordid>3147703</sourcerecordid><originalsourceid>FETCH-LOGICAL-c495t-d04b144036c268d291061c08f3a3db262e535d411549e0ed81fc726163f673d63</originalsourceid><addsrcrecordid>eNqFkctv1DAYxC0EotvCmQtCFodKHNJ-fsROKnEoy6OVKvbA42qc2CleEjvEDqL96-vVrrrAhdNnyb8ZzWgQekbghIBkp6PX8YRIBgJqAvAALUh-FILX8BAtAKgsKk75ATqMcQ0AdVnBY3RAaM2gBligb29cGNxgk2vxarrW3t3q5II_w6s26dGOyRmLP9m-K85jtEPT32DnU8AftQ9pbmzEocNf3aR7vNRjdKbo3Q-L32ZPH7PRE_So0320T3f3CH15_-7z8qK4Wn24XJ5fFS2vy1QY4A3hHJhoqagMzW0EaaHqmGamoYLakpWGE1Ly2oI1FelaSQURrBOSGcGO0Out7zg3gzWt9SlnUuPkBj3dqKCd-vvHu-_qOvxSpGYlr7L-eKefws_ZxqQGF1vb99rbMEclmQQmJc_gy3_AdZgnn7spCoSVVMpNmtMt1E4hxsl290EIqM1yarOc2i-XFS_-zL_nd1Nl4NUO2Cj3dtmvyoeWlermvk_2d8os_g-bkedbZB1TmO4ZRrjMRdkdzC62jw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201352776</pqid></control><display><type>article</type><title>Biomimetic Organization: Octapeptide Self-Assembly into Nanotubes of Viral Capsid-like Dimension</title><source>MEDLINE</source><source>Jstor Complete Legacy</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Valéry, Céline ; Paternostre, Maïté ; Robert, Bruno ; Gulik-Krzywicki, Thaddée ; Narayanan, Theyencheri ; Dedieu, Jean-Claude ; Keller, Gérard ; Torres, Maria-Luisa ; Cherif-Cheikh, Roland ; Calvo, Pilar ; Artzner, Franck</creator><creatorcontrib>Valéry, Céline ; Paternostre, Maïté ; Robert, Bruno ; Gulik-Krzywicki, Thaddée ; Narayanan, Theyencheri ; Dedieu, Jean-Claude ; Keller, Gérard ; Torres, Maria-Luisa ; Cherif-Cheikh, Roland ; Calvo, Pilar ; Artzner, Franck</creatorcontrib><description>The controlled self-assembly of complex molecules into well defined hierarchical structures is a promising route for fabricating nanostructures. These nanoscale structures can be realized by naturally occurring proteins such as tobacco mosaic virus, capsid proteins, tubulin, actin, etc. Here, we report a simple alternative method based on self-assembling nanotubes formed by a synthetic therapeutic octapeptide, Lanreotide in water. We used a multidisciplinary approach involving optical and electron microscopies, vibrational spectroscopies, and small and wide angle x-ray scattering to elucidate the hierarchy of structures exhibited by this system. The results revealed the hexagonal packing of nanotubes, and high degree of monodispersity in the tube diameter (244 Å) and wall thickness (≈18 Å). Moreover, the diameter is tunable by suitable modifications in the molecular structure. The self-assembly of the nanotubes occurs through the association of β-sheets driven by amphiphilicity and a systematic aromatic/aliphatic side chain segregation. This original and simple system is a unique example for the study of complex self-assembling processes generated by de novo molecules or amyloid peptides.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1730609100</identifier><identifier>PMID: 12930900</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Acetates ; Biological Sciences ; Biomimetics ; Biophysics ; Capsid - chemistry ; Disulfides ; Electron density ; Hydrogen bonds ; Models, Molecular ; Molecular structure ; Molecules ; Nanotubes ; Peptides ; Peptides, Cyclic - chemistry ; Protein Conformation ; Protein Structure, Secondary ; Self assembly ; Somatostatin - analogs & derivatives ; Somatostatin - chemistry ; Vibration ; Wave diffraction</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2003-09, Vol.100 (18), p.10258-10262</ispartof><rights>Copyright 1993-2003 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Sep 2, 2003</rights><rights>Copyright © 2003, The National Academy of Sciences 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c495t-d04b144036c268d291061c08f3a3db262e535d411549e0ed81fc726163f673d63</citedby><cites>FETCH-LOGICAL-c495t-d04b144036c268d291061c08f3a3db262e535d411549e0ed81fc726163f673d63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/100/18.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3147703$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3147703$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,724,777,781,800,882,27905,27906,53772,53774,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12930900$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Valéry, Céline</creatorcontrib><creatorcontrib>Paternostre, Maïté</creatorcontrib><creatorcontrib>Robert, Bruno</creatorcontrib><creatorcontrib>Gulik-Krzywicki, Thaddée</creatorcontrib><creatorcontrib>Narayanan, Theyencheri</creatorcontrib><creatorcontrib>Dedieu, Jean-Claude</creatorcontrib><creatorcontrib>Keller, Gérard</creatorcontrib><creatorcontrib>Torres, Maria-Luisa</creatorcontrib><creatorcontrib>Cherif-Cheikh, Roland</creatorcontrib><creatorcontrib>Calvo, Pilar</creatorcontrib><creatorcontrib>Artzner, Franck</creatorcontrib><title>Biomimetic Organization: Octapeptide Self-Assembly into Nanotubes of Viral Capsid-like Dimension</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The controlled self-assembly of complex molecules into well defined hierarchical structures is a promising route for fabricating nanostructures. These nanoscale structures can be realized by naturally occurring proteins such as tobacco mosaic virus, capsid proteins, tubulin, actin, etc. Here, we report a simple alternative method based on self-assembling nanotubes formed by a synthetic therapeutic octapeptide, Lanreotide in water. We used a multidisciplinary approach involving optical and electron microscopies, vibrational spectroscopies, and small and wide angle x-ray scattering to elucidate the hierarchy of structures exhibited by this system. The results revealed the hexagonal packing of nanotubes, and high degree of monodispersity in the tube diameter (244 Å) and wall thickness (≈18 Å). Moreover, the diameter is tunable by suitable modifications in the molecular structure. The self-assembly of the nanotubes occurs through the association of β-sheets driven by amphiphilicity and a systematic aromatic/aliphatic side chain segregation. This original and simple system is a unique example for the study of complex self-assembling processes generated by de novo molecules or amyloid peptides.</description><subject>Acetates</subject><subject>Biological Sciences</subject><subject>Biomimetics</subject><subject>Biophysics</subject><subject>Capsid - chemistry</subject><subject>Disulfides</subject><subject>Electron density</subject><subject>Hydrogen bonds</subject><subject>Models, Molecular</subject><subject>Molecular structure</subject><subject>Molecules</subject><subject>Nanotubes</subject><subject>Peptides</subject><subject>Peptides, Cyclic - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Self assembly</subject><subject>Somatostatin - analogs & derivatives</subject><subject>Somatostatin - chemistry</subject><subject>Vibration</subject><subject>Wave diffraction</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctv1DAYxC0EotvCmQtCFodKHNJ-fsROKnEoy6OVKvbA42qc2CleEjvEDqL96-vVrrrAhdNnyb8ZzWgQekbghIBkp6PX8YRIBgJqAvAALUh-FILX8BAtAKgsKk75ATqMcQ0AdVnBY3RAaM2gBligb29cGNxgk2vxarrW3t3q5II_w6s26dGOyRmLP9m-K85jtEPT32DnU8AftQ9pbmzEocNf3aR7vNRjdKbo3Q-L32ZPH7PRE_So0320T3f3CH15_-7z8qK4Wn24XJ5fFS2vy1QY4A3hHJhoqagMzW0EaaHqmGamoYLakpWGE1Ly2oI1FelaSQURrBOSGcGO0Out7zg3gzWt9SlnUuPkBj3dqKCd-vvHu-_qOvxSpGYlr7L-eKefws_ZxqQGF1vb99rbMEclmQQmJc_gy3_AdZgnn7spCoSVVMpNmtMt1E4hxsl290EIqM1yarOc2i-XFS_-zL_nd1Nl4NUO2Cj3dtmvyoeWlermvk_2d8os_g-bkedbZB1TmO4ZRrjMRdkdzC62jw</recordid><startdate>20030902</startdate><enddate>20030902</enddate><creator>Valéry, Céline</creator><creator>Paternostre, Maïté</creator><creator>Robert, Bruno</creator><creator>Gulik-Krzywicki, Thaddée</creator><creator>Narayanan, Theyencheri</creator><creator>Dedieu, Jean-Claude</creator><creator>Keller, Gérard</creator><creator>Torres, Maria-Luisa</creator><creator>Cherif-Cheikh, Roland</creator><creator>Calvo, Pilar</creator><creator>Artzner, Franck</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20030902</creationdate><title>Biomimetic Organization: Octapeptide Self-Assembly into Nanotubes of Viral Capsid-like Dimension</title><author>Valéry, Céline ; Paternostre, Maïté ; Robert, Bruno ; Gulik-Krzywicki, Thaddée ; Narayanan, Theyencheri ; Dedieu, Jean-Claude ; Keller, Gérard ; Torres, Maria-Luisa ; Cherif-Cheikh, Roland ; Calvo, Pilar ; Artzner, Franck</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c495t-d04b144036c268d291061c08f3a3db262e535d411549e0ed81fc726163f673d63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acetates</topic><topic>Biological Sciences</topic><topic>Biomimetics</topic><topic>Biophysics</topic><topic>Capsid - chemistry</topic><topic>Disulfides</topic><topic>Electron density</topic><topic>Hydrogen bonds</topic><topic>Models, Molecular</topic><topic>Molecular structure</topic><topic>Molecules</topic><topic>Nanotubes</topic><topic>Peptides</topic><topic>Peptides, Cyclic - chemistry</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Self assembly</topic><topic>Somatostatin - analogs & derivatives</topic><topic>Somatostatin - chemistry</topic><topic>Vibration</topic><topic>Wave diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Valéry, Céline</creatorcontrib><creatorcontrib>Paternostre, Maïté</creatorcontrib><creatorcontrib>Robert, Bruno</creatorcontrib><creatorcontrib>Gulik-Krzywicki, Thaddée</creatorcontrib><creatorcontrib>Narayanan, Theyencheri</creatorcontrib><creatorcontrib>Dedieu, Jean-Claude</creatorcontrib><creatorcontrib>Keller, Gérard</creatorcontrib><creatorcontrib>Torres, Maria-Luisa</creatorcontrib><creatorcontrib>Cherif-Cheikh, Roland</creatorcontrib><creatorcontrib>Calvo, Pilar</creatorcontrib><creatorcontrib>Artzner, Franck</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Valéry, Céline</au><au>Paternostre, Maïté</au><au>Robert, Bruno</au><au>Gulik-Krzywicki, Thaddée</au><au>Narayanan, Theyencheri</au><au>Dedieu, Jean-Claude</au><au>Keller, Gérard</au><au>Torres, Maria-Luisa</au><au>Cherif-Cheikh, Roland</au><au>Calvo, Pilar</au><au>Artzner, Franck</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biomimetic Organization: Octapeptide Self-Assembly into Nanotubes of Viral Capsid-like Dimension</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2003-09-02</date><risdate>2003</risdate><volume>100</volume><issue>18</issue><spage>10258</spage><epage>10262</epage><pages>10258-10262</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The controlled self-assembly of complex molecules into well defined hierarchical structures is a promising route for fabricating nanostructures. These nanoscale structures can be realized by naturally occurring proteins such as tobacco mosaic virus, capsid proteins, tubulin, actin, etc. Here, we report a simple alternative method based on self-assembling nanotubes formed by a synthetic therapeutic octapeptide, Lanreotide in water. We used a multidisciplinary approach involving optical and electron microscopies, vibrational spectroscopies, and small and wide angle x-ray scattering to elucidate the hierarchy of structures exhibited by this system. The results revealed the hexagonal packing of nanotubes, and high degree of monodispersity in the tube diameter (244 Å) and wall thickness (≈18 Å). Moreover, the diameter is tunable by suitable modifications in the molecular structure. The self-assembly of the nanotubes occurs through the association of β-sheets driven by amphiphilicity and a systematic aromatic/aliphatic side chain segregation. This original and simple system is a unique example for the study of complex self-assembling processes generated by de novo molecules or amyloid peptides.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>12930900</pmid><doi>10.1073/pnas.1730609100</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2003-09, Vol.100 (18), p.10258-10262 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_proquest_journals_201352776 |
| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Acetates Biological Sciences Biomimetics Biophysics Capsid - chemistry Disulfides Electron density Hydrogen bonds Models, Molecular Molecular structure Molecules Nanotubes Peptides Peptides, Cyclic - chemistry Protein Conformation Protein Structure, Secondary Self assembly Somatostatin - analogs & derivatives Somatostatin - chemistry Vibration Wave diffraction |
| title | Biomimetic Organization: Octapeptide Self-Assembly into Nanotubes of Viral Capsid-like Dimension |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T09%3A34%3A54IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Biomimetic%20Organization:%20Octapeptide%20Self-Assembly%20into%20Nanotubes%20of%20Viral%20Capsid-like%20Dimension&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Val%C3%A9ry,%20C%C3%A9line&rft.date=2003-09-02&rft.volume=100&rft.issue=18&rft.spage=10258&rft.epage=10262&rft.pages=10258-10262&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.1730609100&rft_dat=%3Cjstor_proqu%3E3147703%3C/jstor_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201352776&rft_id=info:pmid/12930900&rft_jstor_id=3147703&rfr_iscdi=true |