Electrochemical studies of the reaction between albumin and amaranth and its analytical application

Sun, Wei; Jiao, Kui; Wang, Xueliang; Lu, Lude

doi:10.1016/j.jelechem.2004.11.042

Cited by 40 publications

(28 citation statements)

References 32 publications

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“…The changes of electrochemical responses of STDs in the presence and absence of HSA showed the interactions of STDs with HSA to form the HSA-mSTD complexes. There may be three different explanations for the decreases at the reductive peak currents of STDs in the presence of HSA: 66,67 (1) the competitive adsorption between the STDs and HSA; (2) the formation of an electrochemically active compound and changes of the electrochemical parameters; (3) the formation of electroinactive complex without the changes of the electrochemical parameters. On the other hand, an adsorbable substance acts usually as an inhibitor of an electrode reaction and shifts reduction process to negative potential.…”

Section: The Voltammetric Behaviour Of Hsa At Physiological Phmentioning

confidence: 99%

Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

Özdemír

Bíçer

2016

J. Chil. Chem. Soc.

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The temperature dependence of the interactions between some steroids (fusidic acid, ouabain and ethynodioldiacetate) and human serum albumin (HSA) at physiological pH (7.4) were studied systematically by square-wave voltammetry. Also, these interactions were proven by means of UV-Vis. absorption spectroscopy and FT-IR spectroscopy techniques. The interaction parameters (binding constants and stoichiometries) at temperature range of 297.5-312.5 K were determined from electrochemical data. It is worthy that the temperature has played a positive role on the interactions of fusidic acid with HSA; however it has negative effective on the interaction parameters of HSA with ouabain or ethynodioldiacetate.

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Section: The Voltammetric Behaviour Of Hsa At Physiological Phmentioning

confidence: 99%

Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

Özdemír

Bíçer

2016

J. Chil. Chem. Soc.

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“…There may be three different explanations for the de- crease of the reductive peak currents after the reaction of fenoprofen with BSA [12]: (1) the competitive adsorption between the fenoprofen and BSA; (2) the formation of an electrochemically active compound and changes of the electrochemical parameters; (3) the formation of electro-inactive complex without the changes of the electrochemical parameters. The shifting in the potential of fenoprofen to more negative values by the addition of BSA could be an evidence for the exclusion of the presence of competitive adsorption on the electrode surface.…”

Section: Affinity Voltammetry Of Fenoprofen-bsamentioning

confidence: 99%

Using of <i>In-Situ</i> Mercury Film Sensor Hyphenated with Affinity Voltammetry for High Throughput Drug-Protein Binding Studies

Youssef¹,

El‐Hady²

2013

AJAC

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A new simple and reliable in-situ mercury film sensor coupled with affinity differential pulse stripping voltammetry (ADSPV) or affinity cyclic voltammetry (ACV) was investigated. The interaction of fenoprofen with bovine serum albumin (BSA) onto the proposed electrochemical sensor was studied. The nature of the electrochemical process of fenoprofen by cyclic voltammetry was depicted. Reproducibility of the proposed method was checked giving a precision of 0.073 standard deviation. The limit of detection and limit of quantification were 7.0 and 22.0 nmol/L, respectively. Fenoprofen was interacted with BSA by 1:1 stoichiometry to form electroinactive supramolecular complex. The binding constant was precisely estimated by non-linear regression analysis based on the shifting of analyte peak potentials. The proposed experiments and data analysis could be used to investigate the drug-protein binding constant within a short analysis time compared to other chromatographic techniques.

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“…Antibodies are commonly used in the development of biosensors for the binding affinity with small molecules 8,10 . Nowadays, the interactions of small molecules such as organic dyes, drugs, and toxic substances with bio-molecules have aroused great interest among chemists and biologists 11,12 . Studies on this type of the interactions are very useful for understanding their structure and functions 11,12 .…”

Section: Introductionmentioning

confidence: 99%

“…Nowadays, the interactions of small molecules such as organic dyes, drugs, and toxic substances with bio-molecules have aroused great interest among chemists and biologists 11,12 . Studies on this type of the interactions are very useful for understanding their structure and functions 11,12 . Electrochemical methods are useful techniques for the study of the interaction of small molecules with biomolecules 11,12 .…”

Section: Introductionmentioning

confidence: 99%

A Voltammetric Study on the Interaction of Novobiocin With Cysteine

Bçer

Qetnkaya

2009

J. Chil. Chem. Soc.

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The interaction of novobiocin (NOV), an aminocoumarin antibiotic, with cysteine was studied by square-wave voltammetry technique on the hanging mercury drop electrode in different pH values. After the addition of NOV into the cysteine solution, the peak current of mercurous cysteine thiolate decreased and its voltammetric peak potential shifted to more positive values. Voltammetric results showed that NOV binds with cysteine forming 1:1 nonelectroactive molecular complex by means of electrostatic and hydrogen-bonding interactions. The binding constants of NOV with cysteine at pHs 5, 7 and 10 were calculated to be 3.06×10 3 , 1.54×10 4 and 1.06×10 5 M -1 , respectively. Furthermore, a possible mechanism of such interaction was also discussed.

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Electrochemical studies of the reaction between albumin and amaranth and its analytical application

Cited by 40 publications

References 32 publications

Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

Using of <i>In-Situ</i> Mercury Film Sensor Hyphenated with Affinity Voltammetry for High Throughput Drug-Protein Binding Studies

A Voltammetric Study on the Interaction of Novobiocin With Cysteine

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Electrochemical studies of the reaction between albumin and amaranth and its analytical application

Cited by 40 publications

References 32 publications

Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

Temperature Effect on Binding Affinity and Stoichiometry Between Some Steroids and Human Serum Albumin

Using of &lt;i&gt;In-Situ&lt;/i&gt; Mercury Film Sensor Hyphenated with Affinity Voltammetry for High Throughput Drug-Protein Binding Studies

A Voltammetric Study on the Interaction of Novobiocin With Cysteine

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Using of <i>In-Situ</i> Mercury Film Sensor Hyphenated with Affinity Voltammetry for High Throughput Drug-Protein Binding Studies