β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction

Detalhes bibliográficos
Autor(a) principal: Milagre, Cíntia D. F. [UNESP]
Data de Publicação: 2012
Outros Autores: Cabeça, Luís F., Almeida, Wanda P., Marsaioli, Anita J.
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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spelling 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:29462023-11-12T06:08:12Repositório 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
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