Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation

Autores
Vico, Raquel Viviana; Voskuhl, Jens; Ravoo, Bart Jan
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
An artificial glycocalix self-assembles when unilamellar bilayer vesicles of amphiphilic β-cyclodextrins are decorated with maltose-and lactose-adamantane conjugates by host-guest interactions. The maltose-decorated vesicles aggregate in the presence of lectin concanavalin A whereas the lactose-decorated vesicles aggregate in the presence of lectin peanut agglutinin. The kinetics of the orthogonal multivalent interfacial interactions present in this ternary system of vesicles, carbohydrates, and lectins were studied by time-dependent measurements of the optical density at 400 nm. The average vesicle and vesicle aggregate sizes were monitored by dynamic light scattering. The aggregation process was evaluated as a function of lectin concentration, vesicle concentration, and surface coverage of the vesicles by the carbohydrate-adamantane conjugates. The initial rate of vesicle aggregation scales linearly with the lectin as well as the cyclodextrin vesicle concentration. Furthermore, each lectin requires a characteristic critical density of carbohydrates at the vesicle surface. These observations allow a prediction of the response of the ternary supramolecular system at different concentrations of its components. Also, the effective binding site separation in a multivalent receptor such as a multiple binding site protein can be accurately determined. This methodology can be extended to multivalent noncovalent interactions in other ligand-receptor systems at interfaces. © 2010 American Chemical Society.
Fil: Vico, Raquel Viviana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Fil: Voskuhl, Jens. Westfalische Wilhelms Universitat; Alemania
Fil: Ravoo, Bart Jan. Westfalische Wilhelms Universitat; Alemania
Materia
CYCLODEXTRIN
CARBOHYDRATES
LECTINS
MULTIVALENCY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/67369
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/67369
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigationVico, Raquel VivianaVoskuhl, JensRavoo, Bart JanCYCLODEXTRINCARBOHYDRATESLECTINSMULTIVALENCYhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1An artificial glycocalix self-assembles when unilamellar bilayer vesicles of amphiphilic β-cyclodextrins are decorated with maltose-and lactose-adamantane conjugates by host-guest interactions. The maltose-decorated vesicles aggregate in the presence of lectin concanavalin A whereas the lactose-decorated vesicles aggregate in the presence of lectin peanut agglutinin. The kinetics of the orthogonal multivalent interfacial interactions present in this ternary system of vesicles, carbohydrates, and lectins were studied by time-dependent measurements of the optical density at 400 nm. The average vesicle and vesicle aggregate sizes were monitored by dynamic light scattering. The aggregation process was evaluated as a function of lectin concentration, vesicle concentration, and surface coverage of the vesicles by the carbohydrate-adamantane conjugates. The initial rate of vesicle aggregation scales linearly with the lectin as well as the cyclodextrin vesicle concentration. Furthermore, each lectin requires a characteristic critical density of carbohydrates at the vesicle surface. These observations allow a prediction of the response of the ternary supramolecular system at different concentrations of its components. Also, the effective binding site separation in a multivalent receptor such as a multiple binding site protein can be accurately determined. This methodology can be extended to multivalent noncovalent interactions in other ligand-receptor systems at interfaces. © 2010 American Chemical Society.Fil: Vico, Raquel Viviana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; ArgentinaFil: Voskuhl, Jens. Westfalische Wilhelms Universitat; AlemaniaFil: Ravoo, Bart Jan. Westfalische Wilhelms Universitat; AlemaniaAmerican Chemical Society2011-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/67369Vico, Raquel Viviana; Voskuhl, Jens; Ravoo, Bart Jan; Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation; American Chemical Society; Langmuir; 27; 4; 2-2011; 1391-13970743-7463CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/la1038975info:eu-repo/semantics/altIdentifier/doi/10.1021/la1038975info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:18:57Zoai:ri.conicet.gov.ar:11336/67369instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:18:57.692CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation
title Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation
spellingShingle Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation
Vico, Raquel Viviana
CYCLODEXTRIN
CARBOHYDRATES
LECTINS
MULTIVALENCY
title_short Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation
title_full Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation
title_fullStr Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation
title_full_unstemmed Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation
title_sort Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation
dc.creator.none.fl_str_mv Vico, Raquel Viviana
Voskuhl, Jens
Ravoo, Bart Jan
author Vico, Raquel Viviana
author_facet Vico, Raquel Viviana
Voskuhl, Jens
Ravoo, Bart Jan
author_role author
author2 Voskuhl, Jens
Ravoo, Bart Jan
author2_role author
author
dc.subject.none.fl_str_mv CYCLODEXTRIN
CARBOHYDRATES
LECTINS
MULTIVALENCY
topic CYCLODEXTRIN
CARBOHYDRATES
LECTINS
MULTIVALENCY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv An artificial glycocalix self-assembles when unilamellar bilayer vesicles of amphiphilic β-cyclodextrins are decorated with maltose-and lactose-adamantane conjugates by host-guest interactions. The maltose-decorated vesicles aggregate in the presence of lectin concanavalin A whereas the lactose-decorated vesicles aggregate in the presence of lectin peanut agglutinin. The kinetics of the orthogonal multivalent interfacial interactions present in this ternary system of vesicles, carbohydrates, and lectins were studied by time-dependent measurements of the optical density at 400 nm. The average vesicle and vesicle aggregate sizes were monitored by dynamic light scattering. The aggregation process was evaluated as a function of lectin concentration, vesicle concentration, and surface coverage of the vesicles by the carbohydrate-adamantane conjugates. The initial rate of vesicle aggregation scales linearly with the lectin as well as the cyclodextrin vesicle concentration. Furthermore, each lectin requires a characteristic critical density of carbohydrates at the vesicle surface. These observations allow a prediction of the response of the ternary supramolecular system at different concentrations of its components. Also, the effective binding site separation in a multivalent receptor such as a multiple binding site protein can be accurately determined. This methodology can be extended to multivalent noncovalent interactions in other ligand-receptor systems at interfaces. © 2010 American Chemical Society.
Fil: Vico, Raquel Viviana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Fil: Voskuhl, Jens. Westfalische Wilhelms Universitat; Alemania
Fil: Ravoo, Bart Jan. Westfalische Wilhelms Universitat; Alemania
description An artificial glycocalix self-assembles when unilamellar bilayer vesicles of amphiphilic β-cyclodextrins are decorated with maltose-and lactose-adamantane conjugates by host-guest interactions. The maltose-decorated vesicles aggregate in the presence of lectin concanavalin A whereas the lactose-decorated vesicles aggregate in the presence of lectin peanut agglutinin. The kinetics of the orthogonal multivalent interfacial interactions present in this ternary system of vesicles, carbohydrates, and lectins were studied by time-dependent measurements of the optical density at 400 nm. The average vesicle and vesicle aggregate sizes were monitored by dynamic light scattering. The aggregation process was evaluated as a function of lectin concentration, vesicle concentration, and surface coverage of the vesicles by the carbohydrate-adamantane conjugates. The initial rate of vesicle aggregation scales linearly with the lectin as well as the cyclodextrin vesicle concentration. Furthermore, each lectin requires a characteristic critical density of carbohydrates at the vesicle surface. These observations allow a prediction of the response of the ternary supramolecular system at different concentrations of its components. Also, the effective binding site separation in a multivalent receptor such as a multiple binding site protein can be accurately determined. This methodology can be extended to multivalent noncovalent interactions in other ligand-receptor systems at interfaces. © 2010 American Chemical Society.
publishDate 2011
dc.date.none.fl_str_mv 2011-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/67369
Vico, Raquel Viviana; Voskuhl, Jens; Ravoo, Bart Jan; Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation; American Chemical Society; Langmuir; 27; 4; 2-2011; 1391-1397
0743-7463
CONICET Digital
CONICET
url http://hdl.handle.net/11336/67369
identifier_str_mv Vico, Raquel Viviana; Voskuhl, Jens; Ravoo, Bart Jan; Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: A kinetic investigation; American Chemical Society; Langmuir; 27; 4; 2-2011; 1391-1397
0743-7463
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/la1038975
info:eu-repo/semantics/altIdentifier/doi/10.1021/la1038975
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844614156831948800
score 13.070432

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