β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1590/S0103-50532012000300005 http://hdl.handle.net/11449/73279 |
Resumo: | Molecular recognition events are key issues in many biological processes. STD NMR (saturation transfer difference nuclear magnetic resonance spectroscopy) is one of the techniques used to understand such biological interactions. Herein, we have investigated the interactions of four β-lactam antibiotics belonging to two classes (cephalosporins and penicillins) with human serum albumin (HSA) by 1H STD NMR revealing that the interaction between the aromatic moiety and HSA is responsible for the binding efficiency. Thus, the structural differences from the five to six-membered thio ring in penicillins and cephalosporins do not seem to influence antibiotic-albumin interactions. © 2012 Sociedade Brasileira de Química. |
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β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interactionβ-lactam antibioticsAlbuminLigand-macromolecules interactionSTD NMRMolecular recognition events are key issues in many biological processes. STD NMR (saturation transfer difference nuclear magnetic resonance spectroscopy) is one of the techniques used to understand such biological interactions. Herein, we have investigated the interactions of four β-lactam antibiotics belonging to two classes (cephalosporins and penicillins) with human serum albumin (HSA) by 1H STD NMR revealing that the interaction between the aromatic moiety and HSA is responsible for the binding efficiency. Thus, the structural differences from the five to six-membered thio ring in penicillins and cephalosporins do not seem to influence antibiotic-albumin interactions. © 2012 Sociedade Brasileira de Química.Institute of Chemistry University of Campinas, CP 6154, 13083-970 Campinas-SPDepartment of Biochemistry and Microbiology Institute of Biosciences Universidade Estadual Paulista, Av. 24A, 1515 Bela Vista, 13506-900 Rio Claro-SPEmbrapa Instrumentação Agropecuária, Rua XV de Novembro, 1452, 13560-970 São Carlos-SPDepartment of Biochemistry and Microbiology Institute of Biosciences Universidade Estadual Paulista, Av. 24A, 1515 Bela Vista, 13506-900 Rio Claro-SPUniversidade Estadual de Campinas (UNICAMP)Universidade Estadual Paulista (Unesp)Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)Milagre, Cíntia D. F. [UNESP]Cabeça, Luís F.Almeida, Wanda P.Marsaioli, Anita J.2014-05-27T11:26:26Z2014-05-27T11:26:26Z2012-04-02info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article403-408application/pdfhttp://dx.doi.org/10.1590/S0103-50532012000300005Journal of the Brazilian Chemical Society, v. 23, n. 3, p. 403-408, 2012.0103-50531678-4790http://hdl.handle.net/11449/7327910.1590/S0103-50532012000300005S0103-505320120003000052-s2.0-848590519782-s2.0-84859051978.pdf14257489168493760000-0001-5627-8616Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of the Brazilian Chemical Society1.4440,3570,357info:eu-repo/semantics/openAccess2023-11-12T06:08:12Zoai:repositorio.unesp.br:11449/73279Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T17:25:53.939208Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction |
title |
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction |
spellingShingle |
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction Milagre, Cíntia D. F. [UNESP] β-lactam antibiotics Albumin Ligand-macromolecules interaction STD NMR |
title_short |
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction |
title_full |
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction |
title_fullStr |
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction |
title_full_unstemmed |
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction |
title_sort |
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction |
author |
Milagre, Cíntia D. F. [UNESP] |
author_facet |
Milagre, Cíntia D. F. [UNESP] Cabeça, Luís F. Almeida, Wanda P. Marsaioli, Anita J. |
author_role |
author |
author2 |
Cabeça, Luís F. Almeida, Wanda P. Marsaioli, Anita J. |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual de Campinas (UNICAMP) Universidade Estadual Paulista (Unesp) Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA) |
dc.contributor.author.fl_str_mv |
Milagre, Cíntia D. F. [UNESP] Cabeça, Luís F. Almeida, Wanda P. Marsaioli, Anita J. |
dc.subject.por.fl_str_mv |
β-lactam antibiotics Albumin Ligand-macromolecules interaction STD NMR |
topic |
β-lactam antibiotics Albumin Ligand-macromolecules interaction STD NMR |
description |
Molecular recognition events are key issues in many biological processes. STD NMR (saturation transfer difference nuclear magnetic resonance spectroscopy) is one of the techniques used to understand such biological interactions. Herein, we have investigated the interactions of four β-lactam antibiotics belonging to two classes (cephalosporins and penicillins) with human serum albumin (HSA) by 1H STD NMR revealing that the interaction between the aromatic moiety and HSA is responsible for the binding efficiency. Thus, the structural differences from the five to six-membered thio ring in penicillins and cephalosporins do not seem to influence antibiotic-albumin interactions. © 2012 Sociedade Brasileira de Química. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-04-02 2014-05-27T11:26:26Z 2014-05-27T11:26:26Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1590/S0103-50532012000300005 Journal of the Brazilian Chemical Society, v. 23, n. 3, p. 403-408, 2012. 0103-5053 1678-4790 http://hdl.handle.net/11449/73279 10.1590/S0103-50532012000300005 S0103-50532012000300005 2-s2.0-84859051978 2-s2.0-84859051978.pdf 1425748916849376 0000-0001-5627-8616 |
url |
http://dx.doi.org/10.1590/S0103-50532012000300005 http://hdl.handle.net/11449/73279 |
identifier_str_mv |
Journal of the Brazilian Chemical Society, v. 23, n. 3, p. 403-408, 2012. 0103-5053 1678-4790 10.1590/S0103-50532012000300005 S0103-50532012000300005 2-s2.0-84859051978 2-s2.0-84859051978.pdf 1425748916849376 0000-0001-5627-8616 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of the Brazilian Chemical Society 1.444 0,357 0,357 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
403-408 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128810012377088 |