Voltammetric studies on the interaction of orange G with proteins: analytical applications

The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA)...

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Main Authors: Sun Wei, Han Junying, Ren Yong, Jiao Kui
Format: Article
Language:English
Published: Sociedade Brasileira de Química 2006-01-01
Series:Journal of the Brazilian Chemical Society
Subjects:
Online Access:http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012
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spelling doaj-da500cb5b88b4ff4af27e9d27a17f97d2020-11-24T22:27:13ZengSociedade Brasileira de QuímicaJournal of the Brazilian Chemical Society0103-50531678-47902006-01-01173510517Voltammetric studies on the interaction of orange G with proteins: analytical applicationsSun WeiHan JunyingRen YongJiao KuiThe interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012orange Ghuman serum albuminvoltammetryinteractionsupramolecule
collection DOAJ
language English
format Article
sources DOAJ
author Sun Wei
Han Junying
Ren Yong
Jiao Kui
spellingShingle Sun Wei
Han Junying
Ren Yong
Jiao Kui
Voltammetric studies on the interaction of orange G with proteins: analytical applications
Journal of the Brazilian Chemical Society
orange G
human serum albumin
voltammetry
interaction
supramolecule
author_facet Sun Wei
Han Junying
Ren Yong
Jiao Kui
author_sort Sun Wei
title Voltammetric studies on the interaction of orange G with proteins: analytical applications
title_short Voltammetric studies on the interaction of orange G with proteins: analytical applications
title_full Voltammetric studies on the interaction of orange G with proteins: analytical applications
title_fullStr Voltammetric studies on the interaction of orange G with proteins: analytical applications
title_full_unstemmed Voltammetric studies on the interaction of orange G with proteins: analytical applications
title_sort voltammetric studies on the interaction of orange g with proteins: analytical applications
publisher Sociedade Brasileira de Química
series Journal of the Brazilian Chemical Society
issn 0103-5053
1678-4790
publishDate 2006-01-01
description The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L-1, 4.0~30.0 mg L-1, 2.0~20.0 mg L-1, 2.0~25.0 mg L-1, 2.0~30.0 mg L-1, respectively. The detection limit was 3.0 mg L-1 for HSA, 3.5 mg L-1 for BSA, 1.0 mg L-1 for OVA, BHb and lipase. The new established electrochemical method was applied to determine the content of albumin in healthy human serum samples and the results were in good agreement with the traditional Coomassie Brilliant Blue (GBB G-250) spectrophotometric method.
topic orange G
human serum albumin
voltammetry
interaction
supramolecule
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532006000300012
work_keys_str_mv AT sunwei voltammetricstudiesontheinteractionoforangegwithproteinsanalyticalapplications
AT hanjunying voltammetricstudiesontheinteractionoforangegwithproteinsanalyticalapplications
AT renyong voltammetricstudiesontheinteractionoforangegwithproteinsanalyticalapplications
AT jiaokui voltammetricstudiesontheinteractionoforangegwithproteinsanalyticalapplications
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