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Silica microspheres functionalized with the iminodiacetic acid/copper(II) complex as a peroxidase mimic for use in metal affinity chromatography-based colorimetric determination of histidine-tagged proteins
Monodisperse porous silica microspheres were functionalized with the iminodiacetic acid/copper(II) complex and then evaluated as a group-specific peroxidase-mimicking nanozyme for colorimetric determination of histidine-tagged (His-tagged) proteins. The green fluorescent protein (GFP) was selected a...
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| Published in: | Mikrochimica acta (1966) 2020-02, Vol.187 (2), p.121-121, Article 121 |
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| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c411t-1d5d1537816f26192b1f1a76f0e4d1abf85b31babba8b1689e62f2fe4099af643 |
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| cites | cdi_FETCH-LOGICAL-c411t-1d5d1537816f26192b1f1a76f0e4d1abf85b31babba8b1689e62f2fe4099af643 |
| container_end_page | 121 |
| container_issue | 2 |
| container_start_page | 121 |
| container_title | Mikrochimica acta (1966) |
| container_volume | 187 |
| creator | Gökçal, Burcu Kip, Çiğdem Şahinbaş, Dilek Çelik, Eda Tuncel, Ali |
| description | Monodisperse porous silica microspheres were functionalized with the iminodiacetic acid/copper(II) complex and then evaluated as a group-specific peroxidase-mimicking nanozyme for colorimetric determination of histidine-tagged (His-tagged) proteins. The green fluorescent protein (GFP) was selected as a typical His-tagged protein. The specificity for GFP and the peroxidase-like activity for the selected substrate were obtained by immobilizing the complex on the porous microspheres. The modified microspheres were also evaluated as a group specific immobilized metal affinity chromatography (IMAC) sorbent for the purification of GFP from
Escherichia coli
extract. The peroxidase-like activity of the microspheres was inhibited by the GFP adsorbed onto the microspheres due to the interaction of His-tagged protein with the immobilized Cu(II) complex. Ortho-phenylenediamine is used as a substrate for the enzyme mimic. The photometric response (measured at 416 nm) is linear in the 9.0–92 μg·mL
−1
GFP concentration range in
E. coli
lysate. The limit of detection is 6.9 μg·mL
−1
.
Graphical abstract
Schematic representation of metal affinity chromatography-based colorimetric determination of histidine-tagged proteins using silica microspheres functionalized with iminodiacteic acid/copper (II) complex as a peroxidase mimic. |
| doi_str_mv | 10.1007/s00604-019-4087-0 |
| format | article |
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Escherichia coli
extract. The peroxidase-like activity of the microspheres was inhibited by the GFP adsorbed onto the microspheres due to the interaction of His-tagged protein with the immobilized Cu(II) complex. Ortho-phenylenediamine is used as a substrate for the enzyme mimic. The photometric response (measured at 416 nm) is linear in the 9.0–92 μg·mL
−1
GFP concentration range in
E. coli
lysate. The limit of detection is 6.9 μg·mL
−1
.
Graphical abstract
Schematic representation of metal affinity chromatography-based colorimetric determination of histidine-tagged proteins using silica microspheres functionalized with iminodiacteic acid/copper (II) complex as a peroxidase mimic.</description><identifier>ISSN: 0026-3672</identifier><identifier>EISSN: 1436-5073</identifier><identifier>DOI: 10.1007/s00604-019-4087-0</identifier><identifier>PMID: 31927641</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Affinity ; Analytical Chemistry ; Characterization and Evaluation of Materials ; Chemistry ; Chemistry and Materials Science ; Chromatography ; Colorimetry ; Coordination compounds ; Copper ; Copper compounds ; E coli ; Escherichia coli ; Evaluation ; Fluorescence ; Histidine ; Microengineering ; Microspheres ; Nanochemistry ; Nanotechnology ; Original Paper ; Peroxidase ; Phenylenediamine ; Proteins ; Silica ; Silicon dioxide ; Sorbents ; Substrates</subject><ispartof>Mikrochimica acta (1966), 2020-02, Vol.187 (2), p.121-121, Article 121</ispartof><rights>Springer-Verlag GmbH Austria, part of Springer Nature 2020</rights><rights>COPYRIGHT 2020 Springer</rights><rights>Springer-Verlag GmbH Austria, part of Springer Nature 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-1d5d1537816f26192b1f1a76f0e4d1abf85b31babba8b1689e62f2fe4099af643</citedby><cites>FETCH-LOGICAL-c411t-1d5d1537816f26192b1f1a76f0e4d1abf85b31babba8b1689e62f2fe4099af643</cites><orcidid>0000-0002-4341-1286</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31927641$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gökçal, Burcu</creatorcontrib><creatorcontrib>Kip, Çiğdem</creatorcontrib><creatorcontrib>Şahinbaş, Dilek</creatorcontrib><creatorcontrib>Çelik, Eda</creatorcontrib><creatorcontrib>Tuncel, Ali</creatorcontrib><title>Silica microspheres functionalized with the iminodiacetic acid/copper(II) complex as a peroxidase mimic for use in metal affinity chromatography-based colorimetric determination of histidine-tagged proteins</title><title>Mikrochimica acta (1966)</title><addtitle>Microchim Acta</addtitle><addtitle>Mikrochim Acta</addtitle><description>Monodisperse porous silica microspheres were functionalized with the iminodiacetic acid/copper(II) complex and then evaluated as a group-specific peroxidase-mimicking nanozyme for colorimetric determination of histidine-tagged (His-tagged) proteins. The green fluorescent protein (GFP) was selected as a typical His-tagged protein. The specificity for GFP and the peroxidase-like activity for the selected substrate were obtained by immobilizing the complex on the porous microspheres. The modified microspheres were also evaluated as a group specific immobilized metal affinity chromatography (IMAC) sorbent for the purification of GFP from
Escherichia coli
extract. The peroxidase-like activity of the microspheres was inhibited by the GFP adsorbed onto the microspheres due to the interaction of His-tagged protein with the immobilized Cu(II) complex. Ortho-phenylenediamine is used as a substrate for the enzyme mimic. The photometric response (measured at 416 nm) is linear in the 9.0–92 μg·mL
−1
GFP concentration range in
E. coli
lysate. The limit of detection is 6.9 μg·mL
−1
.
Graphical abstract
Schematic representation of metal affinity chromatography-based colorimetric determination of histidine-tagged proteins using silica microspheres functionalized with iminodiacteic acid/copper (II) complex as a peroxidase mimic.</description><subject>Affinity</subject><subject>Analytical Chemistry</subject><subject>Characterization and Evaluation of Materials</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chromatography</subject><subject>Colorimetry</subject><subject>Coordination compounds</subject><subject>Copper</subject><subject>Copper compounds</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Evaluation</subject><subject>Fluorescence</subject><subject>Histidine</subject><subject>Microengineering</subject><subject>Microspheres</subject><subject>Nanochemistry</subject><subject>Nanotechnology</subject><subject>Original Paper</subject><subject>Peroxidase</subject><subject>Phenylenediamine</subject><subject>Proteins</subject><subject>Silica</subject><subject>Silicon dioxide</subject><subject>Sorbents</subject><subject>Substrates</subject><issn>0026-3672</issn><issn>1436-5073</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp1ks1u1TAQhSMEopfCA7BBltiURVo7P_bNsqr4uVIlFsA6mtjjG1dJHGxH7eUheSYmSgEJCXlh2f7OmdH4ZNlrwS8F5-oqci55lXPR5BXfq5w_yXaiKmVec1U-zXacFzIvpSrOshcx3nEulCyq59lZKZpCyUrssp9f3OA0sNHp4OPcY8DI7DLp5PwEg_uBht271LPUI3Ojm7xxoDE5zUA7c6X9PGO4OBzeMe3HecAHBpEBo0v_4AxEJGsyZ9YHttDJTWzEBAMDa93k0onpPvgRkj8GmPtT3pHGkNnggyMykNZgwkC1YW2Kect6F5MzbsI8wfFI-Bx8QjfFl9kzC0PEV4_7efbtw_uvN5_y288fDzfXt7muhEi5MLURdan2QtpC0jA6YQUoaTlWRkBn93VXig66DvadkPsGZWELixVvGrCyKs-zi82XCn9fMKZ2dFHjMMCEfoltUZaKK6HUir79B73zS6DZElWpUjWFkCVRlxt1hAFbN1mfAmhaBml6fkLr6P5aiZrXqmo4CcQmWP8tBrTtTPOCcGoFb9d0tFs6WkpHu6ajXTVvHltZuhHNH8XvOBBQbECkp-mI4W-v_3f9BXoIyfY</recordid><startdate>20200201</startdate><enddate>20200201</enddate><creator>Gökçal, Burcu</creator><creator>Kip, Çiğdem</creator><creator>Şahinbaş, Dilek</creator><creator>Çelik, Eda</creator><creator>Tuncel, Ali</creator><general>Springer Vienna</general><general>Springer</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>K9.</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-4341-1286</orcidid></search><sort><creationdate>20200201</creationdate><title>Silica microspheres functionalized with the iminodiacetic acid/copper(II) complex as a peroxidase mimic for use in metal affinity chromatography-based colorimetric determination of histidine-tagged proteins</title><author>Gökçal, Burcu ; Kip, Çiğdem ; Şahinbaş, Dilek ; Çelik, Eda ; Tuncel, Ali</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-1d5d1537816f26192b1f1a76f0e4d1abf85b31babba8b1689e62f2fe4099af643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Affinity</topic><topic>Analytical Chemistry</topic><topic>Characterization and Evaluation of Materials</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chromatography</topic><topic>Colorimetry</topic><topic>Coordination compounds</topic><topic>Copper</topic><topic>Copper compounds</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Evaluation</topic><topic>Fluorescence</topic><topic>Histidine</topic><topic>Microengineering</topic><topic>Microspheres</topic><topic>Nanochemistry</topic><topic>Nanotechnology</topic><topic>Original Paper</topic><topic>Peroxidase</topic><topic>Phenylenediamine</topic><topic>Proteins</topic><topic>Silica</topic><topic>Silicon dioxide</topic><topic>Sorbents</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gökçal, Burcu</creatorcontrib><creatorcontrib>Kip, Çiğdem</creatorcontrib><creatorcontrib>Şahinbaş, Dilek</creatorcontrib><creatorcontrib>Çelik, Eda</creatorcontrib><creatorcontrib>Tuncel, Ali</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Mikrochimica acta (1966)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gökçal, Burcu</au><au>Kip, Çiğdem</au><au>Şahinbaş, Dilek</au><au>Çelik, Eda</au><au>Tuncel, Ali</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Silica microspheres functionalized with the iminodiacetic acid/copper(II) complex as a peroxidase mimic for use in metal affinity chromatography-based colorimetric determination of histidine-tagged proteins</atitle><jtitle>Mikrochimica acta (1966)</jtitle><stitle>Microchim Acta</stitle><addtitle>Mikrochim Acta</addtitle><date>2020-02-01</date><risdate>2020</risdate><volume>187</volume><issue>2</issue><spage>121</spage><epage>121</epage><pages>121-121</pages><artnum>121</artnum><issn>0026-3672</issn><eissn>1436-5073</eissn><abstract>Monodisperse porous silica microspheres were functionalized with the iminodiacetic acid/copper(II) complex and then evaluated as a group-specific peroxidase-mimicking nanozyme for colorimetric determination of histidine-tagged (His-tagged) proteins. The green fluorescent protein (GFP) was selected as a typical His-tagged protein. The specificity for GFP and the peroxidase-like activity for the selected substrate were obtained by immobilizing the complex on the porous microspheres. The modified microspheres were also evaluated as a group specific immobilized metal affinity chromatography (IMAC) sorbent for the purification of GFP from
Escherichia coli
extract. The peroxidase-like activity of the microspheres was inhibited by the GFP adsorbed onto the microspheres due to the interaction of His-tagged protein with the immobilized Cu(II) complex. Ortho-phenylenediamine is used as a substrate for the enzyme mimic. The photometric response (measured at 416 nm) is linear in the 9.0–92 μg·mL
−1
GFP concentration range in
E. coli
lysate. The limit of detection is 6.9 μg·mL
−1
.
Graphical abstract
Schematic representation of metal affinity chromatography-based colorimetric determination of histidine-tagged proteins using silica microspheres functionalized with iminodiacteic acid/copper (II) complex as a peroxidase mimic.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>31927641</pmid><doi>10.1007/s00604-019-4087-0</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-4341-1286</orcidid></addata></record> |
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| ispartof | Mikrochimica acta (1966), 2020-02, Vol.187 (2), p.121-121, Article 121 |
| issn | 0026-3672 1436-5073 |
| language | eng |
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| subjects | Affinity Analytical Chemistry Characterization and Evaluation of Materials Chemistry Chemistry and Materials Science Chromatography Colorimetry Coordination compounds Copper Copper compounds E coli Escherichia coli Evaluation Fluorescence Histidine Microengineering Microspheres Nanochemistry Nanotechnology Original Paper Peroxidase Phenylenediamine Proteins Silica Silicon dioxide Sorbents Substrates |
| title | Silica microspheres functionalized with the iminodiacetic acid/copper(II) complex as a peroxidase mimic for use in metal affinity chromatography-based colorimetric determination of histidine-tagged proteins |
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