Immobilization of recognition elements on a self-assembled monolayers bio-platform

Tailored materials formed by spontaneous two-dimensional arrangement of 3-aminopropyltriethoxysilane self-assembled monolayer on glass (amino-functionalized glass) has been exploited to attach biomolecules in well-organized structures useful in biosensing.  Succinimidyl ester of both unpolymerized d...

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Autores:
Reyes-Cuellar, Julia Constanza
Tipo de recurso:
Article of journal
Fecha de publicación:
2017
Institución:
Universidad Nacional de Colombia
Repositorio:
Universidad Nacional de Colombia
Idioma:
spa
OAI Identifier:
oai:repositorio.unal.edu.co:unal/60370
Acceso en línea:
https://repositorio.unal.edu.co/handle/unal/60370
http://bdigital.unal.edu.co/58702/
Palabra clave:
62 Ingeniería y operaciones afines / Engineering
functionalized surface
biosensor
polydiacetylene liposome
biotin-streptavidin
3-aminopropyltriethoxysilane
superficie funcionalizada
biosensor
liposomas de polidiacetileno
biotina-estreptavidina
aminopropiltrietoxisilano
Rights
openAccess
License
Atribución-NoComercial 4.0 Internacional
id UNACIONAL2_1015361f1a7d540cb11b8acb6c4597a4
oai_identifier_str oai:repositorio.unal.edu.co:unal/60370
network_acronym_str UNACIONAL2
network_name_str Universidad Nacional de Colombia
repository_id_str
dc.title.spa.fl_str_mv Immobilization of recognition elements on a self-assembled monolayers bio-platform
title Immobilization of recognition elements on a self-assembled monolayers bio-platform
spellingShingle Immobilization of recognition elements on a self-assembled monolayers bio-platform
62 Ingeniería y operaciones afines / Engineering
functionalized surface
biosensor
polydiacetylene liposome
biotin-streptavidin
3-aminopropyltriethoxysilane
superficie funcionalizada
biosensor
liposomas de polidiacetileno
biotina-estreptavidina
aminopropiltrietoxisilano
title_short Immobilization of recognition elements on a self-assembled monolayers bio-platform
title_full Immobilization of recognition elements on a self-assembled monolayers bio-platform
title_fullStr Immobilization of recognition elements on a self-assembled monolayers bio-platform
title_full_unstemmed Immobilization of recognition elements on a self-assembled monolayers bio-platform
title_sort Immobilization of recognition elements on a self-assembled monolayers bio-platform
dc.creator.fl_str_mv Reyes-Cuellar, Julia Constanza
dc.contributor.author.spa.fl_str_mv Reyes-Cuellar, Julia Constanza
dc.subject.ddc.spa.fl_str_mv 62 Ingeniería y operaciones afines / Engineering
topic 62 Ingeniería y operaciones afines / Engineering
functionalized surface
biosensor
polydiacetylene liposome
biotin-streptavidin
3-aminopropyltriethoxysilane
superficie funcionalizada
biosensor
liposomas de polidiacetileno
biotina-estreptavidina
aminopropiltrietoxisilano
dc.subject.proposal.spa.fl_str_mv functionalized surface
biosensor
polydiacetylene liposome
biotin-streptavidin
3-aminopropyltriethoxysilane
superficie funcionalizada
biosensor
liposomas de polidiacetileno
biotina-estreptavidina
aminopropiltrietoxisilano
description Tailored materials formed by spontaneous two-dimensional arrangement of 3-aminopropyltriethoxysilane self-assembled monolayer on glass (amino-functionalized glass) has been exploited to attach biomolecules in well-organized structures useful in biosensing.  Succinimidyl ester of both unpolymerized diacetylene liposome (NHS-DA-liposome) layer and PEGylated biotin (Bt-PEG-NHS) matrix were covalently bonded to the amino-functionalized glass by the NHS linker, and exposed to either Tyrosinase (Ty) or Streptavidin (SAV) solution. The interaction between Ty and polymerized NHS-PDA-liposome transformed the planarity of the PDA backbone, and a blue-to-red transition occurred; Bt-PEG attached to the fluorescent-SAV by bioaffinity.  Sensing capability of bioplatform systems was evaluated by Uv-vis spectroscopy or fluorescence microscopy. Biomolecule functionalized SAMs retained the recognition potential of colorimetric Ty-PDA-liposome after biological interaction, and also facilitated the fabrication of a protein-resistant matrix with a particular affinity property.  This surface chemistry is accessible to depositing proteins on both SAM-coated glass surface, and tethered to SAM, resulting in optical bioplatform arrays.
publishDate 2017
dc.date.issued.spa.fl_str_mv 2017-07-01
dc.date.accessioned.spa.fl_str_mv 2019-07-02T18:09:46Z
dc.date.available.spa.fl_str_mv 2019-07-02T18:09:46Z
dc.type.spa.fl_str_mv Artículo de revista
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dc.type.driver.spa.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.issn.spa.fl_str_mv ISSN: 2346-2183
dc.identifier.uri.none.fl_str_mv https://repositorio.unal.edu.co/handle/unal/60370
dc.identifier.eprints.spa.fl_str_mv http://bdigital.unal.edu.co/58702/
identifier_str_mv ISSN: 2346-2183
url https://repositorio.unal.edu.co/handle/unal/60370
http://bdigital.unal.edu.co/58702/
dc.language.iso.spa.fl_str_mv spa
language spa
dc.relation.spa.fl_str_mv https://revistas.unal.edu.co/index.php/dyna/article/view/63963
dc.relation.ispartof.spa.fl_str_mv Universidad Nacional de Colombia Revistas electrónicas UN Dyna
Dyna
dc.relation.references.spa.fl_str_mv Reyes-Cuellar, Julia Constanza (2017) Immobilization of recognition elements on a self-assembled monolayers bio-platform. DYNA, 84 (202). pp. 263-269. ISSN 2346-2183
dc.rights.spa.fl_str_mv Derechos reservados - Universidad Nacional de Colombia
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.license.spa.fl_str_mv Atribución-NoComercial 4.0 Internacional
dc.rights.uri.spa.fl_str_mv http://creativecommons.org/licenses/by-nc/4.0/
dc.rights.accessrights.spa.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv Atribución-NoComercial 4.0 Internacional
Derechos reservados - Universidad Nacional de Colombia
http://creativecommons.org/licenses/by-nc/4.0/
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Universidad Nacional de Colombia (Sede Medellín). Facultad de Minas.
institution Universidad Nacional de Colombia
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spelling Atribución-NoComercial 4.0 InternacionalDerechos reservados - Universidad Nacional de Colombiahttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Reyes-Cuellar, Julia Constanzae1a407ec-4f57-431a-b372-10b90617add93002019-07-02T18:09:46Z2019-07-02T18:09:46Z2017-07-01ISSN: 2346-2183https://repositorio.unal.edu.co/handle/unal/60370http://bdigital.unal.edu.co/58702/Tailored materials formed by spontaneous two-dimensional arrangement of 3-aminopropyltriethoxysilane self-assembled monolayer on glass (amino-functionalized glass) has been exploited to attach biomolecules in well-organized structures useful in biosensing.  Succinimidyl ester of both unpolymerized diacetylene liposome (NHS-DA-liposome) layer and PEGylated biotin (Bt-PEG-NHS) matrix were covalently bonded to the amino-functionalized glass by the NHS linker, and exposed to either Tyrosinase (Ty) or Streptavidin (SAV) solution. The interaction between Ty and polymerized NHS-PDA-liposome transformed the planarity of the PDA backbone, and a blue-to-red transition occurred; Bt-PEG attached to the fluorescent-SAV by bioaffinity.  Sensing capability of bioplatform systems was evaluated by Uv-vis spectroscopy or fluorescence microscopy. Biomolecule functionalized SAMs retained the recognition potential of colorimetric Ty-PDA-liposome after biological interaction, and also facilitated the fabrication of a protein-resistant matrix with a particular affinity property.  This surface chemistry is accessible to depositing proteins on both SAM-coated glass surface, and tethered to SAM, resulting in optical bioplatform arrays.Los materiales funcionalizados por adsorción sobre capas autoensambladas de 3-aminopropiltrietoxisilano (APTS) en vidrio (vidrio amino-funcionalizado) sirven para inmovilizar biomoléculas en estructuras usadas para biosensores.  Liposomas de polidiacetileno (lip-PDA-NHS) y Biotin PEGilado con NHS se inmovilizaron aprovechando el éster de succinimidilo; y sirvieron para reconocer Tirosinasa o streptavidina (SAV). Debido a la interacción liposoma-PDA-Ty, ocurrió un cambio en la planaridad de la cadena polimérica PDA, percibido como una transición de azul-a-rojo; mientras que, la biotina inmovilizada interactúo con SAV por afinidad biológica.  La capacidad de detección del sistema se evaluó por espectroscopia UV-vis o por microscopia de fluorescencia.  Las capas de APTS funcionalizadas con biomoléculas retuvieron la capacidad de reconocimiento colorimétrico después de la interacción biológica, permitiendo la fabricación de una matriz resistente a proteínas con una propiedad de bioafinidad.  Esta química de superficies es simple y accesible para la modificación de substratos de vidrio, útiles en arreglos de bioplataformas ópticas.application/pdfspaUniversidad Nacional de Colombia (Sede Medellín). Facultad de Minas.https://revistas.unal.edu.co/index.php/dyna/article/view/63963Universidad Nacional de Colombia Revistas electrónicas UN DynaDynaReyes-Cuellar, Julia Constanza (2017) Immobilization of recognition elements on a self-assembled monolayers bio-platform. DYNA, 84 (202). pp. 263-269. ISSN 2346-218362 Ingeniería y operaciones afines / Engineeringfunctionalized surfacebiosensorpolydiacetylene liposomebiotin-streptavidin3-aminopropyltriethoxysilanesuperficie funcionalizadabiosensorliposomas de polidiacetilenobiotina-estreptavidinaaminopropiltrietoxisilanoImmobilization of recognition elements on a self-assembled monolayers bio-platformArtículo de revistainfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85Texthttp://purl.org/redcol/resource_type/ARTORIGINAL63963-350195-1-PB.pdfapplication/pdf629718https://repositorio.unal.edu.co/bitstream/unal/60370/1/63963-350195-1-PB.pdf19a4c3bbd3e2f69e11b4368937dfd2b4MD51THUMBNAIL63963-350195-1-PB.pdf.jpg63963-350195-1-PB.pdf.jpgGenerated Thumbnailimage/jpeg9564https://repositorio.unal.edu.co/bitstream/unal/60370/2/63963-350195-1-PB.pdf.jpgffa003942fa67b97c67d341689f94ccaMD52unal/60370oai:repositorio.unal.edu.co:unal/603702023-04-06 23:05:46.302Repositorio Institucional Universidad Nacional de Colombiarepositorio_nal@unal.edu.co

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