Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532012000200018 |
Resumo: | In the present study the interactions between paracetamol (PC) and human serum albumin, in non-glycated (HSA) and glycated form (GHSA), were investigated using continuous cyclic voltammetry in acetate buffer pH 7.4. The results showed lack of significant changes in formal potential E0 and electrode reaction constant rate, k s, of PC. The decay in the drug current, after the addition of protein, showed a decrease in free drug concentration and formation of a biocomplex. The contentious coulometry was also used to determine the binding parameters. The binding constant and binding ratio for HSA and GHSA were 2.0×10(4) and 7.8×10³ mol L-1, respectively, and the number of binding was 2:1 for HSA-PC and 1:1 for GHSA-PC. These results were confirmed by UV-Vis spectroscopy. Thus, the new electrochemical analysis method described here provides an easy and fast method for evaluation of drug-protein interactions with significant clinical implication in diabetes. |
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Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical methodcontinuous cyclic voltammetryglycated human serum albuminparacetamolbinding studyIn the present study the interactions between paracetamol (PC) and human serum albumin, in non-glycated (HSA) and glycated form (GHSA), were investigated using continuous cyclic voltammetry in acetate buffer pH 7.4. The results showed lack of significant changes in formal potential E0 and electrode reaction constant rate, k s, of PC. The decay in the drug current, after the addition of protein, showed a decrease in free drug concentration and formation of a biocomplex. The contentious coulometry was also used to determine the binding parameters. The binding constant and binding ratio for HSA and GHSA were 2.0×10(4) and 7.8×10³ mol L-1, respectively, and the number of binding was 2:1 for HSA-PC and 1:1 for GHSA-PC. These results were confirmed by UV-Vis spectroscopy. Thus, the new electrochemical analysis method described here provides an easy and fast method for evaluation of drug-protein interactions with significant clinical implication in diabetes.Sociedade Brasileira de Química2012-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532012000200018Journal of the Brazilian Chemical Society v.23 n.2 2012reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50532012000200018info:eu-repo/semantics/openAccessDaneshegar,ParandisMoosavi-Movahedi,Ali AkbarNorouzi,ParvizGanjali,Mohammad RezaFarhadi,MohammadSheibanid,Nadereng2012-03-02T00:00:00Zoai:scielo:S0103-50532012000200018Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2012-03-02T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method |
title |
Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method |
spellingShingle |
Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method Daneshegar,Parandis continuous cyclic voltammetry glycated human serum albumin paracetamol binding study |
title_short |
Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method |
title_full |
Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method |
title_fullStr |
Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method |
title_full_unstemmed |
Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method |
title_sort |
Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method |
author |
Daneshegar,Parandis |
author_facet |
Daneshegar,Parandis Moosavi-Movahedi,Ali Akbar Norouzi,Parviz Ganjali,Mohammad Reza Farhadi,Mohammad Sheibanid,Nader |
author_role |
author |
author2 |
Moosavi-Movahedi,Ali Akbar Norouzi,Parviz Ganjali,Mohammad Reza Farhadi,Mohammad Sheibanid,Nader |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Daneshegar,Parandis Moosavi-Movahedi,Ali Akbar Norouzi,Parviz Ganjali,Mohammad Reza Farhadi,Mohammad Sheibanid,Nader |
dc.subject.por.fl_str_mv |
continuous cyclic voltammetry glycated human serum albumin paracetamol binding study |
topic |
continuous cyclic voltammetry glycated human serum albumin paracetamol binding study |
description |
In the present study the interactions between paracetamol (PC) and human serum albumin, in non-glycated (HSA) and glycated form (GHSA), were investigated using continuous cyclic voltammetry in acetate buffer pH 7.4. The results showed lack of significant changes in formal potential E0 and electrode reaction constant rate, k s, of PC. The decay in the drug current, after the addition of protein, showed a decrease in free drug concentration and formation of a biocomplex. The contentious coulometry was also used to determine the binding parameters. The binding constant and binding ratio for HSA and GHSA were 2.0×10(4) and 7.8×10³ mol L-1, respectively, and the number of binding was 2:1 for HSA-PC and 1:1 for GHSA-PC. These results were confirmed by UV-Vis spectroscopy. Thus, the new electrochemical analysis method described here provides an easy and fast method for evaluation of drug-protein interactions with significant clinical implication in diabetes. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-02-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532012000200018 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532012000200018 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0103-50532012000200018 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Journal of the Brazilian Chemical Society v.23 n.2 2012 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
_version_ |
1750318173097295872 |