Identificação de microcistina LR ao nível molecular empregando microscopia de força atômica

Microcystins are non-ribosomal peptides that must be detected for its health concern. Here, microcystin LR and its specific antibody were respectively tethered to the substrate and to the tip of an atomic force microscope, after surface functionalization using 3-aminopropyltriethoxysilane and glutaraldehyde. Functionalization was confirmed comparing topographic images taken on bare and modified tips. Force versus distance curves were successfully used to measure the specific antibody-antigen interactions comparing with a control in which microcystin was initially blocked by incubation with free antibodies. The results showed unequivocally the specific recognition of MLR, suggesting that this method could be useful for biosensor development.

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Main Authors: Etchegaray,Augusto, Bueno,Carolina de Castro, Teschke,Omar
Format: Digital revista
Language:Portuguese
Published: Sociedade Brasileira de Química 2010
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422010000900004
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spelling oai:scielo:S0100-404220100009000042011-01-13Identificação de microcistina LR ao nível molecular empregando microscopia de força atômicaEtchegaray,AugustoBueno,Carolina de CastroTeschke,Omar microcystin LR atomic force microscope biosensor development Microcystins are non-ribosomal peptides that must be detected for its health concern. Here, microcystin LR and its specific antibody were respectively tethered to the substrate and to the tip of an atomic force microscope, after surface functionalization using 3-aminopropyltriethoxysilane and glutaraldehyde. Functionalization was confirmed comparing topographic images taken on bare and modified tips. Force versus distance curves were successfully used to measure the specific antibody-antigen interactions comparing with a control in which microcystin was initially blocked by incubation with free antibodies. The results showed unequivocally the specific recognition of MLR, suggesting that this method could be useful for biosensor development.info:eu-repo/semantics/openAccessSociedade Brasileira de QuímicaQuímica Nova v.33 n.9 20102010-01-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422010000900004pt10.1590/S0100-40422010000900004
institution SCIELO
collection OJS
country Brasil
countrycode BR
component Revista
access En linea
databasecode rev-scielo-br
tag revista
region America del Sur
libraryname SciELO
language Portuguese
format Digital
author Etchegaray,Augusto
Bueno,Carolina de Castro
Teschke,Omar
spellingShingle Etchegaray,Augusto
Bueno,Carolina de Castro
Teschke,Omar
Identificação de microcistina LR ao nível molecular empregando microscopia de força atômica
author_facet Etchegaray,Augusto
Bueno,Carolina de Castro
Teschke,Omar
author_sort Etchegaray,Augusto
title Identificação de microcistina LR ao nível molecular empregando microscopia de força atômica
title_short Identificação de microcistina LR ao nível molecular empregando microscopia de força atômica
title_full Identificação de microcistina LR ao nível molecular empregando microscopia de força atômica
title_fullStr Identificação de microcistina LR ao nível molecular empregando microscopia de força atômica
title_full_unstemmed Identificação de microcistina LR ao nível molecular empregando microscopia de força atômica
title_sort identificação de microcistina lr ao nível molecular empregando microscopia de força atômica
description Microcystins are non-ribosomal peptides that must be detected for its health concern. Here, microcystin LR and its specific antibody were respectively tethered to the substrate and to the tip of an atomic force microscope, after surface functionalization using 3-aminopropyltriethoxysilane and glutaraldehyde. Functionalization was confirmed comparing topographic images taken on bare and modified tips. Force versus distance curves were successfully used to measure the specific antibody-antigen interactions comparing with a control in which microcystin was initially blocked by incubation with free antibodies. The results showed unequivocally the specific recognition of MLR, suggesting that this method could be useful for biosensor development.
publisher Sociedade Brasileira de Química
publishDate 2010
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422010000900004
work_keys_str_mv AT etchegarayaugusto identificacaodemicrocistinalraonivelmolecularempregandomicroscopiadeforcaatomica
AT buenocarolinadecastro identificacaodemicrocistinalraonivelmolecularempregandomicroscopiadeforcaatomica
AT teschkeomar identificacaodemicrocistinalraonivelmolecularempregandomicroscopiadeforcaatomica
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