β-lactam antibiotics epitope mapping with STD NMR spectroscopy: A study of drug-human serum albumin interaction
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
27/05/2014
27/05/2014
02/04/2012
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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. |
Formato |
403-408 |
Identificador |
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 |
Idioma(s) |
eng |
Relação |
Journal of the Brazilian Chemical Society |
Direitos |
openAccess |
Palavras-Chave | #β-lactam antibiotics #Albumin #Ligand-macromolecules interaction #STD NMR |
Tipo |
info:eu-repo/semantics/article |