Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10451/41236 |
Resumo: | Background: Unlike the thin homogeneous films that are typical for adhesives produced by humans, biological adhesives present complex hierarchical micro- and nanostructures. Most studies on marine adhesives have focused on permanent adhesives, whereas the nanostructures of nonpermanent, temporary or reversible adhesives have only been examined in some organisms such as marine flatworms, barnacle cyprids, freshwater cnidaria and echinoderms such as sea cucumbers and sea stars. In this study, the first nanoscale characterization of sea urchin temporary adhesives was performed using atomic force microscopy (AFM). Results: The adhesive topography was similar under dry and native (seawater) conditions, which was comprised of a honeycomb-like meshwork of aggregated globular nanostructures. In terms of adhesion forces, higher values were obtained in dry conditions, reaching up to 50 nN. Under native conditions, lower adhesive forces were obtained (up to 500 pN) but the adhesive seemed to behave like a functional amyloid, as evidenced by the recorded characteristic sawtooth force-extension curves and positive thioflavin-T labelling. Conclusion: Our results confirm that like other temporary adhesives, the sea urchin adhesive footprint nanostructure consists of a meshwork of entangled globular nanostructures. Under native conditions, the adhesive footprints of the sea urchin behaved like a functional amyloid, suggesting that among its proteinaceous constituents there are most likely proteins with amyloid quaternary structures or rich in β-sheets. These results extend our knowledge on sea urchin adhesive composition and mechanical properties essential for the engineering of biomimetic adhesives. |
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Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividusadhesive footprintatomic force microscopynanomechanical propertiessea urchintemporary adhesionBackground: Unlike the thin homogeneous films that are typical for adhesives produced by humans, biological adhesives present complex hierarchical micro- and nanostructures. Most studies on marine adhesives have focused on permanent adhesives, whereas the nanostructures of nonpermanent, temporary or reversible adhesives have only been examined in some organisms such as marine flatworms, barnacle cyprids, freshwater cnidaria and echinoderms such as sea cucumbers and sea stars. In this study, the first nanoscale characterization of sea urchin temporary adhesives was performed using atomic force microscopy (AFM). Results: The adhesive topography was similar under dry and native (seawater) conditions, which was comprised of a honeycomb-like meshwork of aggregated globular nanostructures. In terms of adhesion forces, higher values were obtained in dry conditions, reaching up to 50 nN. Under native conditions, lower adhesive forces were obtained (up to 500 pN) but the adhesive seemed to behave like a functional amyloid, as evidenced by the recorded characteristic sawtooth force-extension curves and positive thioflavin-T labelling. Conclusion: Our results confirm that like other temporary adhesives, the sea urchin adhesive footprint nanostructure consists of a meshwork of entangled globular nanostructures. Under native conditions, the adhesive footprints of the sea urchin behaved like a functional amyloid, suggesting that among its proteinaceous constituents there are most likely proteins with amyloid quaternary structures or rich in β-sheets. These results extend our knowledge on sea urchin adhesive composition and mechanical properties essential for the engineering of biomimetic adhesives.Beilstein-InstitutRepositório da Universidade de LisboaViana, Ana SAlmeida dos Santos, Romana2020-01-19T21:06:31Z20182018-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/41236eng2190-428610.3762/bjnano.9.212info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-11-20T17:53:05Zoai:repositorio.ul.pt:10451/41236Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-11-20T17:53:05Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus |
title |
Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus |
spellingShingle |
Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus Viana, Ana S adhesive footprint atomic force microscopy nanomechanical properties sea urchin temporary adhesion |
title_short |
Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus |
title_full |
Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus |
title_fullStr |
Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus |
title_full_unstemmed |
Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus |
title_sort |
Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus |
author |
Viana, Ana S |
author_facet |
Viana, Ana S Almeida dos Santos, Romana |
author_role |
author |
author2 |
Almeida dos Santos, Romana |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Repositório da Universidade de Lisboa |
dc.contributor.author.fl_str_mv |
Viana, Ana S Almeida dos Santos, Romana |
dc.subject.por.fl_str_mv |
adhesive footprint atomic force microscopy nanomechanical properties sea urchin temporary adhesion |
topic |
adhesive footprint atomic force microscopy nanomechanical properties sea urchin temporary adhesion |
description |
Background: Unlike the thin homogeneous films that are typical for adhesives produced by humans, biological adhesives present complex hierarchical micro- and nanostructures. Most studies on marine adhesives have focused on permanent adhesives, whereas the nanostructures of nonpermanent, temporary or reversible adhesives have only been examined in some organisms such as marine flatworms, barnacle cyprids, freshwater cnidaria and echinoderms such as sea cucumbers and sea stars. In this study, the first nanoscale characterization of sea urchin temporary adhesives was performed using atomic force microscopy (AFM). Results: The adhesive topography was similar under dry and native (seawater) conditions, which was comprised of a honeycomb-like meshwork of aggregated globular nanostructures. In terms of adhesion forces, higher values were obtained in dry conditions, reaching up to 50 nN. Under native conditions, lower adhesive forces were obtained (up to 500 pN) but the adhesive seemed to behave like a functional amyloid, as evidenced by the recorded characteristic sawtooth force-extension curves and positive thioflavin-T labelling. Conclusion: Our results confirm that like other temporary adhesives, the sea urchin adhesive footprint nanostructure consists of a meshwork of entangled globular nanostructures. Under native conditions, the adhesive footprints of the sea urchin behaved like a functional amyloid, suggesting that among its proteinaceous constituents there are most likely proteins with amyloid quaternary structures or rich in β-sheets. These results extend our knowledge on sea urchin adhesive composition and mechanical properties essential for the engineering of biomimetic adhesives. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018 2018-01-01T00:00:00Z 2020-01-19T21:06:31Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10451/41236 |
url |
http://hdl.handle.net/10451/41236 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
2190-4286 10.3762/bjnano.9.212 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Beilstein-Institut |
publisher.none.fl_str_mv |
Beilstein-Institut |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
mluisa.alvim@gmail.com |
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1817549058727739392 |