Nanoscale characterization of the temporary adhesive of the sea urchin Paracentrotus lividus

Detalhes bibliográficos
Autor(a) principal: Viana, Ana S
Data de Publicação: 2018
Outros Autores: Almeida dos Santos, Romana
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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spelling 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
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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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