Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme
Autor(a) principal: | |
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Data de Publicação: | 2006 |
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/10316/10368 https://doi.org/10.1021/ac061040+ |
Resumo: | Atomic force microscopy and differential pulse voltammetry were used to characterize the interaction of small highly structured ribozymes with two carbon electrode surfaces. The ribozymes spontaneously self-assemble in two-dimensional networks that cover the entire HOPG surface uniformly. The full-length ribozyme was adsorbed to a lesser extent than a truncated RNA sequence, presumably due to the formation of a more compact overall structure. All four nucleobases composing the ribozyme could be detected by anodic voltammetry on glassy carbon electrodes, and no signals corresponding to free nucleobases were found, indicating the integrity of the ribozyme molecules. Mg2+ cations significantly reduced the adsorption of ribozymes to the surfaces, in agreement with the stabilization of this ribozyme's compact, stable, and tightly folded tertiary structure by Mg2+ ions that could prevent the hydrophobic bases from interacting with the HOPG surface. Treatment with Pb2+ ions, on the other hand, resulted in an increased adsorption of the RNA due to well-known hydrolytic cleavage. The observed dependence of anodic peak currents on different folding states of RNA may provide an attractive method to electrochemically monitor structural changes associated with RNA folding, binding, and catalysis. |
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Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase RibozymeAtomic force microscopy and differential pulse voltammetry were used to characterize the interaction of small highly structured ribozymes with two carbon electrode surfaces. The ribozymes spontaneously self-assemble in two-dimensional networks that cover the entire HOPG surface uniformly. The full-length ribozyme was adsorbed to a lesser extent than a truncated RNA sequence, presumably due to the formation of a more compact overall structure. All four nucleobases composing the ribozyme could be detected by anodic voltammetry on glassy carbon electrodes, and no signals corresponding to free nucleobases were found, indicating the integrity of the ribozyme molecules. Mg2+ cations significantly reduced the adsorption of ribozymes to the surfaces, in agreement with the stabilization of this ribozyme's compact, stable, and tightly folded tertiary structure by Mg2+ ions that could prevent the hydrophobic bases from interacting with the HOPG surface. Treatment with Pb2+ ions, on the other hand, resulted in an increased adsorption of the RNA due to well-known hydrolytic cleavage. The observed dependence of anodic peak currents on different folding states of RNA may provide an attractive method to electrochemically monitor structural changes associated with RNA folding, binding, and catalysis.American Chemical Society2006-12-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/10368http://hdl.handle.net/10316/10368https://doi.org/10.1021/ac061040+engAnalytical Chemistry. 78:24 (2006) 8256-82640003-2700Paquim, A. M. ChiorceaPiedade, J. A. P.Wombacher, R.Jäschke, A.Oliveira-Brett, A. M.info: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:RCAAP2020-05-25T13:13:11Zoai:estudogeral.uc.pt:10316/10368Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:01:14.311560Repositório 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 |
Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme |
title |
Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme |
spellingShingle |
Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme Paquim, A. M. Chiorcea |
title_short |
Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme |
title_full |
Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme |
title_fullStr |
Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme |
title_full_unstemmed |
Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme |
title_sort |
Atomic Force Microscopy and Anodic Voltammetry Characterization of a 49-Mer Diels-Alderase Ribozyme |
author |
Paquim, A. M. Chiorcea |
author_facet |
Paquim, A. M. Chiorcea Piedade, J. A. P. Wombacher, R. Jäschke, A. Oliveira-Brett, A. M. |
author_role |
author |
author2 |
Piedade, J. A. P. Wombacher, R. Jäschke, A. Oliveira-Brett, A. M. |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Paquim, A. M. Chiorcea Piedade, J. A. P. Wombacher, R. Jäschke, A. Oliveira-Brett, A. M. |
description |
Atomic force microscopy and differential pulse voltammetry were used to characterize the interaction of small highly structured ribozymes with two carbon electrode surfaces. The ribozymes spontaneously self-assemble in two-dimensional networks that cover the entire HOPG surface uniformly. The full-length ribozyme was adsorbed to a lesser extent than a truncated RNA sequence, presumably due to the formation of a more compact overall structure. All four nucleobases composing the ribozyme could be detected by anodic voltammetry on glassy carbon electrodes, and no signals corresponding to free nucleobases were found, indicating the integrity of the ribozyme molecules. Mg2+ cations significantly reduced the adsorption of ribozymes to the surfaces, in agreement with the stabilization of this ribozyme's compact, stable, and tightly folded tertiary structure by Mg2+ ions that could prevent the hydrophobic bases from interacting with the HOPG surface. Treatment with Pb2+ ions, on the other hand, resulted in an increased adsorption of the RNA due to well-known hydrolytic cleavage. The observed dependence of anodic peak currents on different folding states of RNA may provide an attractive method to electrochemically monitor structural changes associated with RNA folding, binding, and catalysis. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-12-15 |
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/10316/10368 http://hdl.handle.net/10316/10368 https://doi.org/10.1021/ac061040+ |
url |
http://hdl.handle.net/10316/10368 https://doi.org/10.1021/ac061040+ |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Analytical Chemistry. 78:24 (2006) 8256-8264 0003-2700 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
American Chemical Society |
publisher.none.fl_str_mv |
American Chemical Society |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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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 |
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1799133904761782272 |