An ab initio conformational study on captopril

Autores
Zamarbide, Graciela Nidia; Estrada, Mario Rinaldo; Zamora, Miguel Angel; Torday, Ladislaus L.; Enriz, Ricardo Daniel; Vert, Francisco Tomás; Csizmadia, Imre Gyula
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Captopril can interact regio- and stereo-specifically with various functional groups present at the active site of angiotensin converting enzyme (ACE). Since no X-ray structure of ACE is available, Captopril, as an ACE inhibitor may be used as a 'molecular caliper', to estimate upper and lower bound values for separation d, where the mercaptidic terminal group of the molecule is linked to the enzyme Zn2+ cofactor, while the carboxylate links via an hydrogen bond to the guanidine moiety of an arginine side chain. As the results of this Ab Initio study, the conformations of the dianionic form of the full captopril molecule are reported here.
Fil: Zamarbide, Graciela Nidia. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
Fil: Estrada, Mario Rinaldo. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
Fil: Zamora, Miguel Angel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
Fil: Torday, Ladislaus L.. University of Szeged; Hungría
Fil: Enriz, Ricardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Vert, Francisco Tomás. Universidad de Valencia; España
Fil: Csizmadia, Imre Gyula. University of Toronto; Canadá. University of Szeged; Hungría
Materia
ANTIHYPERTENSIVE DRUG
CAPTOPRIL
MOLECULAR CALIPER
ORGANIC SULPHUR
ROLE OF ZN2+ COFACTOR
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:11336/127402
Acceder
id CONICETDig_12d557ab779d71082f3d590a9d112938
oai_identifier_str oai:ri.conicet.gov.ar:11336/127402
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling An ab initio conformational study on captoprilZamarbide, Graciela NidiaEstrada, Mario RinaldoZamora, Miguel AngelTorday, Ladislaus L.Enriz, Ricardo DanielVert, Francisco TomásCsizmadia, Imre GyulaANTIHYPERTENSIVE DRUGCAPTOPRILMOLECULAR CALIPERORGANIC SULPHURROLE OF ZN2+ COFACTORhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Captopril can interact regio- and stereo-specifically with various functional groups present at the active site of angiotensin converting enzyme (ACE). Since no X-ray structure of ACE is available, Captopril, as an ACE inhibitor may be used as a 'molecular caliper', to estimate upper and lower bound values for separation d, where the mercaptidic terminal group of the molecule is linked to the enzyme Zn2+ cofactor, while the carboxylate links via an hydrogen bond to the guanidine moiety of an arginine side chain. As the results of this Ab Initio study, the conformations of the dianionic form of the full captopril molecule are reported here.Fil: Zamarbide, Graciela Nidia. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; ArgentinaFil: Estrada, Mario Rinaldo. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; ArgentinaFil: Zamora, Miguel Angel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; ArgentinaFil: Torday, Ladislaus L.. University of Szeged; HungríaFil: Enriz, Ricardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Vert, Francisco Tomás. Universidad de Valencia; EspañaFil: Csizmadia, Imre Gyula. University of Toronto; Canadá. University of Szeged; HungríaElsevier Science2003-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/127402Zamarbide, Graciela Nidia; Estrada, Mario Rinaldo; Zamora, Miguel Angel; Torday, Ladislaus L.; Enriz, Ricardo Daniel; et al.; An ab initio conformational study on captopril; Elsevier Science; Journal of Molecular Structure Theochem; 666-667; 12-2003; 599-6080166-1280CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S016612800300719Xinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.theochem.2003.08.084info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:54:21Zoai:ri.conicet.gov.ar:11336/127402instacron: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:34982025-09-03 09:54:21.539CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv An ab initio conformational study on captopril
title An ab initio conformational study on captopril
spellingShingle An ab initio conformational study on captopril
Zamarbide, Graciela Nidia
ANTIHYPERTENSIVE DRUG
CAPTOPRIL
MOLECULAR CALIPER
ORGANIC SULPHUR
ROLE OF ZN2+ COFACTOR
title_short An ab initio conformational study on captopril
title_full An ab initio conformational study on captopril
title_fullStr An ab initio conformational study on captopril
title_full_unstemmed An ab initio conformational study on captopril
title_sort An ab initio conformational study on captopril
dc.creator.none.fl_str_mv Zamarbide, Graciela Nidia
Estrada, Mario Rinaldo
Zamora, Miguel Angel
Torday, Ladislaus L.
Enriz, Ricardo Daniel
Vert, Francisco Tomás
Csizmadia, Imre Gyula
author Zamarbide, Graciela Nidia
author_facet Zamarbide, Graciela Nidia
Estrada, Mario Rinaldo
Zamora, Miguel Angel
Torday, Ladislaus L.
Enriz, Ricardo Daniel
Vert, Francisco Tomás
Csizmadia, Imre Gyula
author_role author
author2 Estrada, Mario Rinaldo
Zamora, Miguel Angel
Torday, Ladislaus L.
Enriz, Ricardo Daniel
Vert, Francisco Tomás
Csizmadia, Imre Gyula
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ANTIHYPERTENSIVE DRUG
CAPTOPRIL
MOLECULAR CALIPER
ORGANIC SULPHUR
ROLE OF ZN2+ COFACTOR
topic ANTIHYPERTENSIVE DRUG
CAPTOPRIL
MOLECULAR CALIPER
ORGANIC SULPHUR
ROLE OF ZN2+ COFACTOR
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Captopril can interact regio- and stereo-specifically with various functional groups present at the active site of angiotensin converting enzyme (ACE). Since no X-ray structure of ACE is available, Captopril, as an ACE inhibitor may be used as a 'molecular caliper', to estimate upper and lower bound values for separation d, where the mercaptidic terminal group of the molecule is linked to the enzyme Zn2+ cofactor, while the carboxylate links via an hydrogen bond to the guanidine moiety of an arginine side chain. As the results of this Ab Initio study, the conformations of the dianionic form of the full captopril molecule are reported here.
Fil: Zamarbide, Graciela Nidia. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
Fil: Estrada, Mario Rinaldo. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
Fil: Zamora, Miguel Angel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
Fil: Torday, Ladislaus L.. University of Szeged; Hungría
Fil: Enriz, Ricardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Vert, Francisco Tomás. Universidad de Valencia; España
Fil: Csizmadia, Imre Gyula. University of Toronto; Canadá. University of Szeged; Hungría
description Captopril can interact regio- and stereo-specifically with various functional groups present at the active site of angiotensin converting enzyme (ACE). Since no X-ray structure of ACE is available, Captopril, as an ACE inhibitor may be used as a 'molecular caliper', to estimate upper and lower bound values for separation d, where the mercaptidic terminal group of the molecule is linked to the enzyme Zn2+ cofactor, while the carboxylate links via an hydrogen bond to the guanidine moiety of an arginine side chain. As the results of this Ab Initio study, the conformations of the dianionic form of the full captopril molecule are reported here.
publishDate 2003
dc.date.none.fl_str_mv 2003-12
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/11336/127402
Zamarbide, Graciela Nidia; Estrada, Mario Rinaldo; Zamora, Miguel Angel; Torday, Ladislaus L.; Enriz, Ricardo Daniel; et al.; An ab initio conformational study on captopril; Elsevier Science; Journal of Molecular Structure Theochem; 666-667; 12-2003; 599-608
0166-1280
CONICET Digital
CONICET
url http://hdl.handle.net/11336/127402
identifier_str_mv Zamarbide, Graciela Nidia; Estrada, Mario Rinaldo; Zamora, Miguel Angel; Torday, Ladislaus L.; Enriz, Ricardo Daniel; et al.; An ab initio conformational study on captopril; Elsevier Science; Journal of Molecular Structure Theochem; 666-667; 12-2003; 599-608
0166-1280
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://www.sciencedirect.com/science/article/abs/pii/S016612800300719X
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.theochem.2003.08.084
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 Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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_ 1842269281108099072
score 13.13397

Publicaciones similares