Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors

Autores
Testero, Sebastian Andres; Lee, Mijoon; Staran, Rachel T.; Espahbodi, Mana; Llarrull, Leticia Irene; Toth, Marta; Mobashery, Shahriar; Chang, Mayland
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Matrix metalloproteinases (MMPs) are important zinc-dependent endopeptidases. Two members of this family of enzymes called gelatinases (MMP-2 and MMP-9) have been implicated in a number of human diseases, including cancer, neurological and cardiovascular diseases, and inflammation, to name a few. We describe in this report the preparation and evaluation of two structural types of thiirane inhibitors that show selectivity toward gelatinases. The biphenyl series targets both gelatinases, whereas the monophenyl analogues exhibit potent inhibition of only MMP-2. The latter structural type also exhibits improved water solubility and metabolic stability, both traits desirable for progress of these molecules forward in gelatinase-dependent animal models of disease.
Fil: Testero, Sebastian Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina. University of Notre Dame; Estados Unidos
Fil: Lee, Mijoon. University of Notre Dame; Estados Unidos
Fil: Staran, Rachel T.. University of Notre Dame; Estados Unidos
Fil: Espahbodi, Mana. University of Notre Dame; Estados Unidos
Fil: Llarrull, Leticia Irene. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. University of Notre Dame; Estados Unidos
Fil: Toth, Marta. University of Notre Dame; Estados Unidos
Fil: Mobashery, Shahriar. University of Notre Dame; Estados Unidos
Fil: Chang, Mayland. University of Notre Dame; Estados Unidos
Materia
MATRIX METALLOPROTEINASES
SLOW-BINDING GELATINASE INHIBITORS
THIIRANES
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:11336/127718
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Sulfonate-Containing Thiiranes as Selective Gelatinase InhibitorsTestero, Sebastian AndresLee, MijoonStaran, Rachel T.Espahbodi, ManaLlarrull, Leticia IreneToth, MartaMobashery, ShahriarChang, MaylandMATRIX METALLOPROTEINASESSLOW-BINDING GELATINASE INHIBITORSTHIIRANEShttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Matrix metalloproteinases (MMPs) are important zinc-dependent endopeptidases. Two members of this family of enzymes called gelatinases (MMP-2 and MMP-9) have been implicated in a number of human diseases, including cancer, neurological and cardiovascular diseases, and inflammation, to name a few. We describe in this report the preparation and evaluation of two structural types of thiirane inhibitors that show selectivity toward gelatinases. The biphenyl series targets both gelatinases, whereas the monophenyl analogues exhibit potent inhibition of only MMP-2. The latter structural type also exhibits improved water solubility and metabolic stability, both traits desirable for progress of these molecules forward in gelatinase-dependent animal models of disease.Fil: Testero, Sebastian Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina. University of Notre Dame; Estados UnidosFil: Lee, Mijoon. University of Notre Dame; Estados UnidosFil: Staran, Rachel T.. University of Notre Dame; Estados UnidosFil: Espahbodi, Mana. University of Notre Dame; Estados UnidosFil: Llarrull, Leticia Irene. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. University of Notre Dame; Estados UnidosFil: Toth, Marta. University of Notre Dame; Estados UnidosFil: Mobashery, Shahriar. University of Notre Dame; Estados UnidosFil: Chang, Mayland. University of Notre Dame; Estados UnidosAmerican Chemical Society2011-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/127718Testero, Sebastian Andres; Lee, Mijoon; Staran, Rachel T.; Espahbodi, Mana; Llarrull, Leticia Irene; et al.; Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors; American Chemical Society; ACS Medicinal Chemistry Letters; 2; 2; 2-2011; 177-1811948-5875CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/ml100254einfo:eu-repo/semantics/altIdentifier/doi/10.1021/ml100254einfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4018095/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 Técnicas2025-09-29T10:44:50Zoai:ri.conicet.gov.ar:11336/127718instacron: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 10:44:51.137CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
title Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
spellingShingle Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
Testero, Sebastian Andres
MATRIX METALLOPROTEINASES
SLOW-BINDING GELATINASE INHIBITORS
THIIRANES
title_short Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
title_full Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
title_fullStr Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
title_full_unstemmed Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
title_sort Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors
dc.creator.none.fl_str_mv Testero, Sebastian Andres
Lee, Mijoon
Staran, Rachel T.
Espahbodi, Mana
Llarrull, Leticia Irene
Toth, Marta
Mobashery, Shahriar
Chang, Mayland
author Testero, Sebastian Andres
author_facet Testero, Sebastian Andres
Lee, Mijoon
Staran, Rachel T.
Espahbodi, Mana
Llarrull, Leticia Irene
Toth, Marta
Mobashery, Shahriar
Chang, Mayland
author_role author
author2 Lee, Mijoon
Staran, Rachel T.
Espahbodi, Mana
Llarrull, Leticia Irene
Toth, Marta
Mobashery, Shahriar
Chang, Mayland
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv MATRIX METALLOPROTEINASES
SLOW-BINDING GELATINASE INHIBITORS
THIIRANES
topic MATRIX METALLOPROTEINASES
SLOW-BINDING GELATINASE INHIBITORS
THIIRANES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Matrix metalloproteinases (MMPs) are important zinc-dependent endopeptidases. Two members of this family of enzymes called gelatinases (MMP-2 and MMP-9) have been implicated in a number of human diseases, including cancer, neurological and cardiovascular diseases, and inflammation, to name a few. We describe in this report the preparation and evaluation of two structural types of thiirane inhibitors that show selectivity toward gelatinases. The biphenyl series targets both gelatinases, whereas the monophenyl analogues exhibit potent inhibition of only MMP-2. The latter structural type also exhibits improved water solubility and metabolic stability, both traits desirable for progress of these molecules forward in gelatinase-dependent animal models of disease.
Fil: Testero, Sebastian Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina. University of Notre Dame; Estados Unidos
Fil: Lee, Mijoon. University of Notre Dame; Estados Unidos
Fil: Staran, Rachel T.. University of Notre Dame; Estados Unidos
Fil: Espahbodi, Mana. University of Notre Dame; Estados Unidos
Fil: Llarrull, Leticia Irene. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. University of Notre Dame; Estados Unidos
Fil: Toth, Marta. University of Notre Dame; Estados Unidos
Fil: Mobashery, Shahriar. University of Notre Dame; Estados Unidos
Fil: Chang, Mayland. University of Notre Dame; Estados Unidos
description Matrix metalloproteinases (MMPs) are important zinc-dependent endopeptidases. Two members of this family of enzymes called gelatinases (MMP-2 and MMP-9) have been implicated in a number of human diseases, including cancer, neurological and cardiovascular diseases, and inflammation, to name a few. We describe in this report the preparation and evaluation of two structural types of thiirane inhibitors that show selectivity toward gelatinases. The biphenyl series targets both gelatinases, whereas the monophenyl analogues exhibit potent inhibition of only MMP-2. The latter structural type also exhibits improved water solubility and metabolic stability, both traits desirable for progress of these molecules forward in gelatinase-dependent animal models of disease.
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/11336/127718
Testero, Sebastian Andres; Lee, Mijoon; Staran, Rachel T.; Espahbodi, Mana; Llarrull, Leticia Irene; et al.; Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors; American Chemical Society; ACS Medicinal Chemistry Letters; 2; 2; 2-2011; 177-181
1948-5875
CONICET Digital
CONICET
url http://hdl.handle.net/11336/127718
identifier_str_mv Testero, Sebastian Andres; Lee, Mijoon; Staran, Rachel T.; Espahbodi, Mana; Llarrull, Leticia Irene; et al.; Sulfonate-Containing Thiiranes as Selective Gelatinase Inhibitors; American Chemical Society; ACS Medicinal Chemistry Letters; 2; 2; 2-2011; 177-181
1948-5875
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/10.1021/ml100254e
info:eu-repo/semantics/altIdentifier/doi/10.1021/ml100254e
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4018095/
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
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_ 1844614486763241472
score 13.070432

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