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

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

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.

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Main Authors: Milagre,Cíntia D. F., Cabeça,Luís F., Almeida,Wanda P., Marsaioli,Anita J.
Format: Digital revista
Language:English
Published: Sociedade Brasileira de Química 2012
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532012000300005
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spelling oai:scielo:S0103-505320120003000052012-04-04β-lactam antibiotics epitope mapping with STD NMR spectroscopy: a study of drug-human serum albumin interactionMilagre,Cíntia D. F.Cabeça,Luís F.Almeida,Wanda P.Marsaioli,Anita J. STD NMR ligand-macromolecules interaction albumin β-lactam antibiotics 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.info:eu-repo/semantics/openAccessSociedade Brasileira de QuímicaJournal of the Brazilian Chemical Society v.23 n.3 20122012-03-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532012000300005en10.1590/S0103-50532012000300005
institution SCIELO
collection OJS
country Brasil
countrycode BR
component Revista
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databasecode rev-scielo-br
tag revista
region America del Sur
libraryname SciELO
language English
format Digital
author Milagre,Cíntia D. F.
Cabeça,Luís F.
Almeida,Wanda P.
Marsaioli,Anita J.
spellingShingle Milagre,Cíntia D. F.
Cabeça,Luís F.
Almeida,Wanda P.
Marsaioli,Anita J.
β-lactam antibiotics epitope mapping with STD NMR spectroscopy: a study of drug-human serum albumin interaction
author_facet Milagre,Cíntia D. F.
Cabeça,Luís F.
Almeida,Wanda P.
Marsaioli,Anita J.
author_sort Milagre,Cíntia D. F.
title β-lactam antibiotics epitope mapping with STD NMR spectroscopy: a study of drug-human serum albumin interaction
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
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.
publisher Sociedade Brasileira de Química
publishDate 2012
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532012000300005
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AT cabecaluisf blactamantibioticsepitopemappingwithstdnmrspectroscopyastudyofdrughumanserumalbumininteraction
AT almeidawandap blactamantibioticsepitopemappingwithstdnmrspectroscopyastudyofdrughumanserumalbumininteraction
AT marsaiolianitaj blactamantibioticsepitopemappingwithstdnmrspectroscopyastudyofdrughumanserumalbumininteraction
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