Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose

Autores
Di Lella, Santiago; Ma, Lu; Diaz Ricci, Juan Carlos; Rabinovich, Gabriel Adrián; Asher, Sanford A.; Alvarez, Rosa Maria Susana
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Galectin-1 (Gal-1), a member of a family of evolutionarily conserved glycan-binding proteins, binds specifically to poly-N-acetyllactosamine-enriched glycoconjugates. Through interactions with these glycoconjugates, this protein modulates inflammatory responses and contributes to tumor progression and immune cell homeostasis. The carbohydrate recognition domain includes the single protein tryptophan (Trp68). UV resonance Raman spectroscopy and molecular dynamic simulation were used to examine the change in the environment of the Trp on ligand binding. The UV Raman spectra and the calculated water radial distribution functions show that, while no large structural changes in the protein follow lactose binding, substantial solvent reorganization occurs. These new insights into the microscopic role of water molecules in Gal-1 binding to its specific carbohydrate ligands provides a better understanding of the physicochemical properties of Gal-1-saccharide interactions, which will be useful for the design of synthetic inhibitors for therapeutic purposes.
Fil: Di Lella, Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Universidad de Buenos Aires; Argentina
Fil: Ma, Lu. University of Pittsburgh; Estados Unidos
Fil: Diaz Ricci, Juan Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Asher, Sanford A.. University of Pittsburgh; Estados Unidos
Fil: Alvarez, Rosa Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
Materia
Galectin-1
Solvent Environment
Lactose Binding
Protein Binding
Lactose Metabolism
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:11336/24819
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/24819
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Critical role of the solvent environment in galectin-1 binding to the disaccharide lactoseDi Lella, SantiagoMa, LuDiaz Ricci, Juan CarlosRabinovich, Gabriel AdriánAsher, Sanford A.Alvarez, Rosa Maria SusanaGalectin-1Solvent EnvironmentLactose BindingProtein BindingLactose Metabolismhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Galectin-1 (Gal-1), a member of a family of evolutionarily conserved glycan-binding proteins, binds specifically to poly-N-acetyllactosamine-enriched glycoconjugates. Through interactions with these glycoconjugates, this protein modulates inflammatory responses and contributes to tumor progression and immune cell homeostasis. The carbohydrate recognition domain includes the single protein tryptophan (Trp68). UV resonance Raman spectroscopy and molecular dynamic simulation were used to examine the change in the environment of the Trp on ligand binding. The UV Raman spectra and the calculated water radial distribution functions show that, while no large structural changes in the protein follow lactose binding, substantial solvent reorganization occurs. These new insights into the microscopic role of water molecules in Gal-1 binding to its specific carbohydrate ligands provides a better understanding of the physicochemical properties of Gal-1-saccharide interactions, which will be useful for the design of synthetic inhibitors for therapeutic purposes.Fil: Di Lella, Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Universidad de Buenos Aires; ArgentinaFil: Ma, Lu. University of Pittsburgh; Estados UnidosFil: Diaz Ricci, Juan Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Asher, Sanford A.. University of Pittsburgh; Estados UnidosFil: Alvarez, Rosa Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; ArgentinaAmerican Chemical Society2009-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/24819Di Lella, Santiago; Ma, Lu; Diaz Ricci, Juan Carlos; Rabinovich, Gabriel Adrián; Asher, Sanford A.; et al.; Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose; American Chemical Society; Biochemistry; 48; 4; 12-2009; 786-7910006-29601520-4995CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/bi801855ginfo:eu-repo/semantics/altIdentifier/doi/10.1021/bi801855ginfo:eu-repo/semantics/altIdentifier/pmid/19128029info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2633424/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:19:34Zoai:ri.conicet.gov.ar:11336/24819instacron: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 10:19:34.781CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
title Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
spellingShingle Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
Di Lella, Santiago
Galectin-1
Solvent Environment
Lactose Binding
Protein Binding
Lactose Metabolism
title_short Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
title_full Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
title_fullStr Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
title_full_unstemmed Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
title_sort Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
dc.creator.none.fl_str_mv Di Lella, Santiago
Ma, Lu
Diaz Ricci, Juan Carlos
Rabinovich, Gabriel Adrián
Asher, Sanford A.
Alvarez, Rosa Maria Susana
author Di Lella, Santiago
author_facet Di Lella, Santiago
Ma, Lu
Diaz Ricci, Juan Carlos
Rabinovich, Gabriel Adrián
Asher, Sanford A.
Alvarez, Rosa Maria Susana
author_role author
author2 Ma, Lu
Diaz Ricci, Juan Carlos
Rabinovich, Gabriel Adrián
Asher, Sanford A.
Alvarez, Rosa Maria Susana
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Galectin-1
Solvent Environment
Lactose Binding
Protein Binding
Lactose Metabolism
topic Galectin-1
Solvent Environment
Lactose Binding
Protein Binding
Lactose Metabolism
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Galectin-1 (Gal-1), a member of a family of evolutionarily conserved glycan-binding proteins, binds specifically to poly-N-acetyllactosamine-enriched glycoconjugates. Through interactions with these glycoconjugates, this protein modulates inflammatory responses and contributes to tumor progression and immune cell homeostasis. The carbohydrate recognition domain includes the single protein tryptophan (Trp68). UV resonance Raman spectroscopy and molecular dynamic simulation were used to examine the change in the environment of the Trp on ligand binding. The UV Raman spectra and the calculated water radial distribution functions show that, while no large structural changes in the protein follow lactose binding, substantial solvent reorganization occurs. These new insights into the microscopic role of water molecules in Gal-1 binding to its specific carbohydrate ligands provides a better understanding of the physicochemical properties of Gal-1-saccharide interactions, which will be useful for the design of synthetic inhibitors for therapeutic purposes.
Fil: Di Lella, Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Universidad de Buenos Aires; Argentina
Fil: Ma, Lu. University of Pittsburgh; Estados Unidos
Fil: Diaz Ricci, Juan Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Asher, Sanford A.. University of Pittsburgh; Estados Unidos
Fil: Alvarez, Rosa Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
description Galectin-1 (Gal-1), a member of a family of evolutionarily conserved glycan-binding proteins, binds specifically to poly-N-acetyllactosamine-enriched glycoconjugates. Through interactions with these glycoconjugates, this protein modulates inflammatory responses and contributes to tumor progression and immune cell homeostasis. The carbohydrate recognition domain includes the single protein tryptophan (Trp68). UV resonance Raman spectroscopy and molecular dynamic simulation were used to examine the change in the environment of the Trp on ligand binding. The UV Raman spectra and the calculated water radial distribution functions show that, while no large structural changes in the protein follow lactose binding, substantial solvent reorganization occurs. These new insights into the microscopic role of water molecules in Gal-1 binding to its specific carbohydrate ligands provides a better understanding of the physicochemical properties of Gal-1-saccharide interactions, which will be useful for the design of synthetic inhibitors for therapeutic purposes.
publishDate 2009
dc.date.none.fl_str_mv 2009-12
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/11336/24819
Di Lella, Santiago; Ma, Lu; Diaz Ricci, Juan Carlos; Rabinovich, Gabriel Adrián; Asher, Sanford A.; et al.; Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose; American Chemical Society; Biochemistry; 48; 4; 12-2009; 786-791
0006-2960
1520-4995
CONICET Digital
CONICET
url http://hdl.handle.net/11336/24819
identifier_str_mv Di Lella, Santiago; Ma, Lu; Diaz Ricci, Juan Carlos; Rabinovich, Gabriel Adrián; Asher, Sanford A.; et al.; Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose; American Chemical Society; Biochemistry; 48; 4; 12-2009; 786-791
0006-2960
1520-4995
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/abs/10.1021/bi801855g
info:eu-repo/semantics/altIdentifier/doi/10.1021/bi801855g
info:eu-repo/semantics/altIdentifier/pmid/19128029
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2633424/
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
application/pdf
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
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score 13.070432

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