The Experts below are selected from a list of 192 Experts worldwide ranked by ideXlab platform
Hanna Radecka - One of the best experts on this subject based on the ideXlab platform.
-
Electrochemical Biosensor for the Detection of Glycated Albumin.
Current Alzheimer research, 2017Co-Authors: Edyta Mikuła, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Aleksandra Wysłouch-cieszyńska, Liliya Zhukova, Hanna RadeckaAbstract:Background: Alzheimer’s disease (AD) is the most common form of dementia. The process of AD can begin 20 years before any symptom of cognitive loss. Thus, the development of systems for early diagnosis and prevention is very important. The mechanism of AD is still under debate. Nevertheless, higher levels of glycated albumin in cerebrospinal fluid and plasma are observed in AD patients. Therefore, glycated albumin could be a biomarker of AD development. Methods: Electrochemical biosensor for direct determination of glycated albumin was based on thiol derivative of Pentetic Acid (DTPA) complex with Cu(II) created on gold electrode surface. His-tagged domains of Receptors for Advanced Glycation End Products (RAGE) were applied as analytical active element for glycated albumin recognition. The binding of glycated albumin by His6- RAGE domains was monitored using Osteryoung square - wave voltammetry. Results: Electrodes modified with His6 - RAGE VC1 natural domain generated decrease of Cu(II) redox currents in the presence of glycated albumin. Human albumin, Aβ 1-40 and S100B protein caused negligible influence on biosensors responses towards glycated albumin. The detection limits were: 2.3 pM, 1.1 pM, 2.9 pM and 3.1 pM in the presence of: buffer, buffer + albumin, buffer + S100B, buffer + Aβ1-40 , respectively. Conclusion: The presented electrochemical biosensor was successfully applied for the determination of glycated albumin. Considering analytical parameters such as good selectivity and sensitivity in pM range, biosensor could be recommended as an analytical tool for medical samples analysis.
-
Voltammetric Detection of S100B Protein Using His-Tagged Receptor Domains for Advanced Glycation End Products (RAGE) Immobilized onto a Gold Electrode Surface
Sensors, 2014Co-Authors: Edyta Mikuła, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Aleksandra Wysłouch-cieszyńska, Liliya Zhukova, M. Puchalska, Hanna RadeckaAbstract:In this work we report on an electrochemical biosensor for the determination of the S100B protein. The His-tagged VC1 domains of Receptors for Advanced Glycation End (RAGE) products used as analytically active molecules were covalently immobilized on a monolayer of a thiol derivative of Pentetic Acid (DPTA) complex with Cu(II) deposited on a gold electrode surface. The recognition processes between the RAGE VC1 domain and the S100B protein results in changes in the redox activity of the DPTA-Cu(II) centres which were measured by Osteryoung square-wave voltammetry (OSWV). In order to verify whether the observed analytical signal originates from the recognition process between the His6–RAGE VC1 domains and the S100B protein, the electrode modified with the His6–RAGE C2 and His6–RAGE VC1 deleted domains which have no ability to bind S100B peptides were applied. The proposed biosensor was quite sensitive, with a detection limit of 0.52 pM recorded in the buffer solution. The presence of diluted human plasma and 10 nM Aβ1-40 have no influence on the biosensor performance.
-
Pentetic Acid dpta cu ii monolayer deposited on gold electrode the base of biosensors for electrochemical screening of kinase jak2 and potential inhibitor interactions
Sensors and Actuators B-chemical, 2014Co-Authors: Justyn Wojtasik, Marcin Mielecki, Katarzyna Kurzątkowska, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2–potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines–isoquinolone alkaloids, as well as caffeic Acid—a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented.
-
Pentetic Acid (DPTA) Cu(II) monolayer deposited on gold electrode—The base of biosensors for electrochemical screening of kinase JAK2 and potential inhibitor interactions
Sensors and Actuators B: Chemical, 2014Co-Authors: Justyn Wojtasik, Marcin Mielecki, Katarzyna Kurzątkowska, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2–potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines–isoquinolone alkaloids, as well as caffeic Acid—a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented.
-
Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes.
Talanta, 2014Co-Authors: Katarzyna Kurzątkowska, Marcin Mielecki, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:New surface plasmon resonance (SPR) sensing platforms which consists of copper (II) complexes of a Pentetic Acid thiol ligand (DPTA-Cu(II)) and of a thiol derivative of dipyrromethene (DPM-Cu(II) created on the surface of gold SPR disc were applied to oriented immobilization of His-tagged Janus kinase 2 (GST-His6-JAK2). This method is based on the covalent bond formation between histidine from a His-tag chain of a protein and Cu(II) centres from the complexes. The kinetic and thermodynamic parameters of the oriented immobilization of GST-His6-JAK2 protein to DPTA-Cu(II) and DPM-Cu(II) complexes attached to the Au surface of a SPR disc were discussed.
Peter Verwilst - One of the best experts on this subject based on the ideXlab platform.
-
Electrochemical Biosensor for the Detection of Glycated Albumin.
Current Alzheimer research, 2017Co-Authors: Edyta Mikuła, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Aleksandra Wysłouch-cieszyńska, Liliya Zhukova, Hanna RadeckaAbstract:Background: Alzheimer’s disease (AD) is the most common form of dementia. The process of AD can begin 20 years before any symptom of cognitive loss. Thus, the development of systems for early diagnosis and prevention is very important. The mechanism of AD is still under debate. Nevertheless, higher levels of glycated albumin in cerebrospinal fluid and plasma are observed in AD patients. Therefore, glycated albumin could be a biomarker of AD development. Methods: Electrochemical biosensor for direct determination of glycated albumin was based on thiol derivative of Pentetic Acid (DTPA) complex with Cu(II) created on gold electrode surface. His-tagged domains of Receptors for Advanced Glycation End Products (RAGE) were applied as analytical active element for glycated albumin recognition. The binding of glycated albumin by His6- RAGE domains was monitored using Osteryoung square - wave voltammetry. Results: Electrodes modified with His6 - RAGE VC1 natural domain generated decrease of Cu(II) redox currents in the presence of glycated albumin. Human albumin, Aβ 1-40 and S100B protein caused negligible influence on biosensors responses towards glycated albumin. The detection limits were: 2.3 pM, 1.1 pM, 2.9 pM and 3.1 pM in the presence of: buffer, buffer + albumin, buffer + S100B, buffer + Aβ1-40 , respectively. Conclusion: The presented electrochemical biosensor was successfully applied for the determination of glycated albumin. Considering analytical parameters such as good selectivity and sensitivity in pM range, biosensor could be recommended as an analytical tool for medical samples analysis.
-
Voltammetric Detection of S100B Protein Using His-Tagged Receptor Domains for Advanced Glycation End Products (RAGE) Immobilized onto a Gold Electrode Surface
Sensors, 2014Co-Authors: Edyta Mikuła, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Aleksandra Wysłouch-cieszyńska, Liliya Zhukova, M. Puchalska, Hanna RadeckaAbstract:In this work we report on an electrochemical biosensor for the determination of the S100B protein. The His-tagged VC1 domains of Receptors for Advanced Glycation End (RAGE) products used as analytically active molecules were covalently immobilized on a monolayer of a thiol derivative of Pentetic Acid (DPTA) complex with Cu(II) deposited on a gold electrode surface. The recognition processes between the RAGE VC1 domain and the S100B protein results in changes in the redox activity of the DPTA-Cu(II) centres which were measured by Osteryoung square-wave voltammetry (OSWV). In order to verify whether the observed analytical signal originates from the recognition process between the His6–RAGE VC1 domains and the S100B protein, the electrode modified with the His6–RAGE C2 and His6–RAGE VC1 deleted domains which have no ability to bind S100B peptides were applied. The proposed biosensor was quite sensitive, with a detection limit of 0.52 pM recorded in the buffer solution. The presence of diluted human plasma and 10 nM Aβ1-40 have no influence on the biosensor performance.
-
Pentetic Acid dpta cu ii monolayer deposited on gold electrode the base of biosensors for electrochemical screening of kinase jak2 and potential inhibitor interactions
Sensors and Actuators B-chemical, 2014Co-Authors: Justyn Wojtasik, Marcin Mielecki, Katarzyna Kurzątkowska, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2–potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines–isoquinolone alkaloids, as well as caffeic Acid—a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented.
-
Pentetic Acid (DPTA) Cu(II) monolayer deposited on gold electrode—The base of biosensors for electrochemical screening of kinase JAK2 and potential inhibitor interactions
Sensors and Actuators B: Chemical, 2014Co-Authors: Justyn Wojtasik, Marcin Mielecki, Katarzyna Kurzątkowska, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2–potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines–isoquinolone alkaloids, as well as caffeic Acid—a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented.
-
Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes.
Talanta, 2014Co-Authors: Katarzyna Kurzątkowska, Marcin Mielecki, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:New surface plasmon resonance (SPR) sensing platforms which consists of copper (II) complexes of a Pentetic Acid thiol ligand (DPTA-Cu(II)) and of a thiol derivative of dipyrromethene (DPM-Cu(II) created on the surface of gold SPR disc were applied to oriented immobilization of His-tagged Janus kinase 2 (GST-His6-JAK2). This method is based on the covalent bond formation between histidine from a His-tag chain of a protein and Cu(II) centres from the complexes. The kinetic and thermodynamic parameters of the oriented immobilization of GST-His6-JAK2 protein to DPTA-Cu(II) and DPM-Cu(II) complexes attached to the Au surface of a SPR disc were discussed.
Jerzy Radecki - One of the best experts on this subject based on the ideXlab platform.
-
Electrochemical Biosensor for the Detection of Glycated Albumin.
Current Alzheimer research, 2017Co-Authors: Edyta Mikuła, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Aleksandra Wysłouch-cieszyńska, Liliya Zhukova, Hanna RadeckaAbstract:Background: Alzheimer’s disease (AD) is the most common form of dementia. The process of AD can begin 20 years before any symptom of cognitive loss. Thus, the development of systems for early diagnosis and prevention is very important. The mechanism of AD is still under debate. Nevertheless, higher levels of glycated albumin in cerebrospinal fluid and plasma are observed in AD patients. Therefore, glycated albumin could be a biomarker of AD development. Methods: Electrochemical biosensor for direct determination of glycated albumin was based on thiol derivative of Pentetic Acid (DTPA) complex with Cu(II) created on gold electrode surface. His-tagged domains of Receptors for Advanced Glycation End Products (RAGE) were applied as analytical active element for glycated albumin recognition. The binding of glycated albumin by His6- RAGE domains was monitored using Osteryoung square - wave voltammetry. Results: Electrodes modified with His6 - RAGE VC1 natural domain generated decrease of Cu(II) redox currents in the presence of glycated albumin. Human albumin, Aβ 1-40 and S100B protein caused negligible influence on biosensors responses towards glycated albumin. The detection limits were: 2.3 pM, 1.1 pM, 2.9 pM and 3.1 pM in the presence of: buffer, buffer + albumin, buffer + S100B, buffer + Aβ1-40 , respectively. Conclusion: The presented electrochemical biosensor was successfully applied for the determination of glycated albumin. Considering analytical parameters such as good selectivity and sensitivity in pM range, biosensor could be recommended as an analytical tool for medical samples analysis.
-
Voltammetric Detection of S100B Protein Using His-Tagged Receptor Domains for Advanced Glycation End Products (RAGE) Immobilized onto a Gold Electrode Surface
Sensors, 2014Co-Authors: Edyta Mikuła, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Aleksandra Wysłouch-cieszyńska, Liliya Zhukova, M. Puchalska, Hanna RadeckaAbstract:In this work we report on an electrochemical biosensor for the determination of the S100B protein. The His-tagged VC1 domains of Receptors for Advanced Glycation End (RAGE) products used as analytically active molecules were covalently immobilized on a monolayer of a thiol derivative of Pentetic Acid (DPTA) complex with Cu(II) deposited on a gold electrode surface. The recognition processes between the RAGE VC1 domain and the S100B protein results in changes in the redox activity of the DPTA-Cu(II) centres which were measured by Osteryoung square-wave voltammetry (OSWV). In order to verify whether the observed analytical signal originates from the recognition process between the His6–RAGE VC1 domains and the S100B protein, the electrode modified with the His6–RAGE C2 and His6–RAGE VC1 deleted domains which have no ability to bind S100B peptides were applied. The proposed biosensor was quite sensitive, with a detection limit of 0.52 pM recorded in the buffer solution. The presence of diluted human plasma and 10 nM Aβ1-40 have no influence on the biosensor performance.
-
Pentetic Acid dpta cu ii monolayer deposited on gold electrode the base of biosensors for electrochemical screening of kinase jak2 and potential inhibitor interactions
Sensors and Actuators B-chemical, 2014Co-Authors: Justyn Wojtasik, Marcin Mielecki, Katarzyna Kurzątkowska, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2–potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines–isoquinolone alkaloids, as well as caffeic Acid—a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented.
-
Pentetic Acid (DPTA) Cu(II) monolayer deposited on gold electrode—The base of biosensors for electrochemical screening of kinase JAK2 and potential inhibitor interactions
Sensors and Actuators B: Chemical, 2014Co-Authors: Justyn Wojtasik, Marcin Mielecki, Katarzyna Kurzątkowska, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2–potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines–isoquinolone alkaloids, as well as caffeic Acid—a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented.
-
Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes.
Talanta, 2014Co-Authors: Katarzyna Kurzątkowska, Marcin Mielecki, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:New surface plasmon resonance (SPR) sensing platforms which consists of copper (II) complexes of a Pentetic Acid thiol ligand (DPTA-Cu(II)) and of a thiol derivative of dipyrromethene (DPM-Cu(II) created on the surface of gold SPR disc were applied to oriented immobilization of His-tagged Janus kinase 2 (GST-His6-JAK2). This method is based on the covalent bond formation between histidine from a His-tag chain of a protein and Cu(II) centres from the complexes. The kinetic and thermodynamic parameters of the oriented immobilization of GST-His6-JAK2 protein to DPTA-Cu(II) and DPM-Cu(II) complexes attached to the Au surface of a SPR disc were discussed.
Wim Dehaen - One of the best experts on this subject based on the ideXlab platform.
-
Electrochemical Biosensor for the Detection of Glycated Albumin.
Current Alzheimer research, 2017Co-Authors: Edyta Mikuła, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Aleksandra Wysłouch-cieszyńska, Liliya Zhukova, Hanna RadeckaAbstract:Background: Alzheimer’s disease (AD) is the most common form of dementia. The process of AD can begin 20 years before any symptom of cognitive loss. Thus, the development of systems for early diagnosis and prevention is very important. The mechanism of AD is still under debate. Nevertheless, higher levels of glycated albumin in cerebrospinal fluid and plasma are observed in AD patients. Therefore, glycated albumin could be a biomarker of AD development. Methods: Electrochemical biosensor for direct determination of glycated albumin was based on thiol derivative of Pentetic Acid (DTPA) complex with Cu(II) created on gold electrode surface. His-tagged domains of Receptors for Advanced Glycation End Products (RAGE) were applied as analytical active element for glycated albumin recognition. The binding of glycated albumin by His6- RAGE domains was monitored using Osteryoung square - wave voltammetry. Results: Electrodes modified with His6 - RAGE VC1 natural domain generated decrease of Cu(II) redox currents in the presence of glycated albumin. Human albumin, Aβ 1-40 and S100B protein caused negligible influence on biosensors responses towards glycated albumin. The detection limits were: 2.3 pM, 1.1 pM, 2.9 pM and 3.1 pM in the presence of: buffer, buffer + albumin, buffer + S100B, buffer + Aβ1-40 , respectively. Conclusion: The presented electrochemical biosensor was successfully applied for the determination of glycated albumin. Considering analytical parameters such as good selectivity and sensitivity in pM range, biosensor could be recommended as an analytical tool for medical samples analysis.
-
Voltammetric Detection of S100B Protein Using His-Tagged Receptor Domains for Advanced Glycation End Products (RAGE) Immobilized onto a Gold Electrode Surface
Sensors, 2014Co-Authors: Edyta Mikuła, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Aleksandra Wysłouch-cieszyńska, Liliya Zhukova, M. Puchalska, Hanna RadeckaAbstract:In this work we report on an electrochemical biosensor for the determination of the S100B protein. The His-tagged VC1 domains of Receptors for Advanced Glycation End (RAGE) products used as analytically active molecules were covalently immobilized on a monolayer of a thiol derivative of Pentetic Acid (DPTA) complex with Cu(II) deposited on a gold electrode surface. The recognition processes between the RAGE VC1 domain and the S100B protein results in changes in the redox activity of the DPTA-Cu(II) centres which were measured by Osteryoung square-wave voltammetry (OSWV). In order to verify whether the observed analytical signal originates from the recognition process between the His6–RAGE VC1 domains and the S100B protein, the electrode modified with the His6–RAGE C2 and His6–RAGE VC1 deleted domains which have no ability to bind S100B peptides were applied. The proposed biosensor was quite sensitive, with a detection limit of 0.52 pM recorded in the buffer solution. The presence of diluted human plasma and 10 nM Aβ1-40 have no influence on the biosensor performance.
-
Pentetic Acid dpta cu ii monolayer deposited on gold electrode the base of biosensors for electrochemical screening of kinase jak2 and potential inhibitor interactions
Sensors and Actuators B-chemical, 2014Co-Authors: Justyn Wojtasik, Marcin Mielecki, Katarzyna Kurzątkowska, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2–potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines–isoquinolone alkaloids, as well as caffeic Acid—a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented.
-
Pentetic Acid (DPTA) Cu(II) monolayer deposited on gold electrode—The base of biosensors for electrochemical screening of kinase JAK2 and potential inhibitor interactions
Sensors and Actuators B: Chemical, 2014Co-Authors: Justyn Wojtasik, Marcin Mielecki, Katarzyna Kurzątkowska, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2–potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines–isoquinolone alkaloids, as well as caffeic Acid—a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented.
-
Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes.
Talanta, 2014Co-Authors: Katarzyna Kurzątkowska, Marcin Mielecki, Krystyna Grzelak, Peter Verwilst, Wim Dehaen, Jerzy Radecki, Hanna RadeckaAbstract:New surface plasmon resonance (SPR) sensing platforms which consists of copper (II) complexes of a Pentetic Acid thiol ligand (DPTA-Cu(II)) and of a thiol derivative of dipyrromethene (DPM-Cu(II) created on the surface of gold SPR disc were applied to oriented immobilization of His-tagged Janus kinase 2 (GST-His6-JAK2). This method is based on the covalent bond formation between histidine from a His-tag chain of a protein and Cu(II) centres from the complexes. The kinetic and thermodynamic parameters of the oriented immobilization of GST-His6-JAK2 protein to DPTA-Cu(II) and DPM-Cu(II) complexes attached to the Au surface of a SPR disc were discussed.
Radecka Hanna - One of the best experts on this subject based on the ideXlab platform.
-
Voltammetric Detection of S100B Protein Using His-Tagged Receptor Domains for Advanced Glycation End Products (RAGE) Immobilized onto a Gold Electrode Surface
'MDPI AG', 2014Co-Authors: Mikula Edyta, Verwilst Peter, Dehaen Wim, Radecki Jerzy, Wyslouch-cieszynska Aleksandra, Zhukova Liliya, Puchalska Monika, Radecka HannaAbstract:In this work we report on an electrochemical biosensor for the determination of the S100B protein. The His-tagged VC1 domains of Receptors for Advanced Glycation End (RAGE) products used as analytically active molecules were covalently immobilized on a monolayer of a thiol derivative of Pentetic Acid (DPTA) complex with Cu(II) deposited on a gold electrode surface. The recognition processes between the RAGE VC1 domain and the S100B protein results in changes in the redox activity of the DPTA-Cu(II) centres which were measured by Osteryoung square-wave voltammetry (OSWV). In order to verify whether the observed analytical signal originates from the recognition process between the His6-RAGE VC1 domains and the S100B protein, the electrode modified with the His6-RAGE C2 and His6-RAGE VC1 deleted domains which have no ability to bind S100B peptides were applied. The proposed biosensor was quite sensitive, with a detection limit of 0.52 pM recorded in the buffer solution. The presence of diluted human plasma and 10 nM Aβ(1-40) have no influence on the biosensor performance.status: publishe
-
Pentetic Acid (DPTA) Cu(II) monolayer deposited on gold electrode-The base of biosensors for electrochemical screening of kinase JAK2 and potential inhibitor interactions
'Elsevier BV', 2014Co-Authors: Wojtasik Justyn, Mielecki Marcin, Kurzatkowska Katarzyna, Grzelak Krystyna, Verwilst Peter, Dehaen Wim, Radecki Jerzy, Radecka HannaAbstract:Here, the new biosensor destined for screening of interactions between kinase JAK2 and compounds which may act as inhibitors was presented. The Cu(II) complex of Pentetic Acid thiol ligand was applied for immobilization of kinase JAK2 on the gold electrode surface through his-tagged chemistry. The base of the biosensor response was the change of the electrochemical properties of the Cu(II) redox centres upon formation of the kinase JAK2-potential inhibitor complex. The increasing inhibitor concentration caused the decrease of reduction/oxidation Cu(II) current observed with Osteryoung square wave voltammetry. The biosensor usability was checked using known inhibitors, berberines-isoquinolone alkaloids, as well as caffeic Acid - a control compound which has no affinity to kinase JAK2. The possible parameters suitable for estimation of the strength of the interactions between kinase JAK2 covalently attached to the Cu(II) complex of Pentetic Acid thiol ligand deposited on the gold electrode surface and potential inhibitors present in the solution were presented. © 2014 Elsevier B.V. All rights reserved.status: publishe
-
Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes
'Elsevier BV', 2014Co-Authors: Kurzatkowska Katarzyna, Mielecki Marcin, Grzelak Krystyna, Verwilst Peter, Dehaen Wim, Radecki Jerzy, Radecka HannaAbstract:New surface plasmon resonance (SPR) sensing platforms which consists of copper (II) complexes of a Pentetic Acid thiol ligand (DPTA-Cu(II)) and of a thiol derivative of dipyrromethene (DPM-Cu(II) created on the surface of gold SPR disc were applied to oriented immobilization of His-tagged Janus kinase 2 (GST-His6-JAK2). This method is based on the covalent bond formation between histidine from a His-tag chain of a protein and Cu(II) centres from the complexes. The kinetic and thermodynamic parameters of the oriented immobilization of GST-His6-JAK2 protein to DPTA-Cu(II) and DPM-Cu(II) complexes attached to the Au surface of a SPR disc were discussed.publisher: Elsevier articletitle: Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes journaltitle: Talanta articlelink: http://dx.doi.org/10.1016/j.talanta.2014.07.013 content_type: article copyright: Copyright © 2014 Elsevier B.V. All rights reserved.status: publishe
-
Oriented Immobilization of His-Tagged Protein on a Redox Active Thiol Derivative of DPTA-Cu(II) Layer Deposited on a Gold Electrode-The Base of Electrochemical Biosensors
'MDPI AG', 2013Co-Authors: Mikula Edyta, Verwilst Peter, Dehaen Wim, Radecki Jerzy, Wyslouch-cieszynska Aleksandra, Sulima Magdalena, Marszalek Ilona, Radecka HannaAbstract:This paper concerns the development of an electrochemical biosensor for the determination of Aβ(16-23') and A(β1-40) peptides. The His-tagged V and VC1 domains of Receptor for Advanced Glycation end Products (RAGE) immobilized on a gold electrode surface were used as analytically active molecules. The immobilization of His6-RAGE domains consists of: (i) formation of a mixed layer of N-acetylcysteamine (NAC) and the thiol derivative of Pentetic Acid (DPTA); (ii) complexation of Cu(II) by DPTA; (iii) oriented immobilization of His6-RAGE domains via coordination bonds between Cu(II) sites from DPTA-Cu(II) complex and imidazole nitrogen atoms of a histidine tag. Each modification step was controlled by cyclic voltammetry (CV), Osteryoung square-wave voltammetry (OSWV), and atomic force microscopy (AFM). The applicability of the proposed biosensor was tested in the presence of human plasma, which had no influence on its performance. The detection limits for Aβ(1-40) determination were 1.06 nM and 0.80 nM, in the presence of buffer and human plasma, respectively. These values reach the concentration level of Aβ(1-40) which is relevant for determination of its soluble form in human plasma, as well as in brain. This indicates the promising future application of biosensor presented for early diagnosis of neurodegenerative diseases.status: publishe