Loading…
Imprinted Fe–Ni double hydroxide nanorods with high selective protein adsorption capacity
Anchoring more template proteins on the carrier surface is one of the most critical steps in the preparation process of protein-imprinted polymers. Inspired by the stable interactions between metal ions and proteins, high external surface iron-nickel double hydroxides (Fe–Ni LDH) derived from metal–...
Saved in:
Published in: | Journal of materials science 2024-11, Vol.59 (42), p.19837-19854 |
---|---|
Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | |
---|---|
cites | cdi_FETCH-LOGICAL-c200t-74ba9c1f9c48136952f8bc10d9b1f8862966fdbbeb2b289943c8d308020a6bd53 |
container_end_page | 19854 |
container_issue | 42 |
container_start_page | 19837 |
container_title | Journal of materials science |
container_volume | 59 |
creator | Wang, Ting Lyu, Yanting Zhao, Kehan Ahmad, Mudasir Zhang, Baoliang |
description | Anchoring more template proteins on the carrier surface is one of the most critical steps in the preparation process of protein-imprinted polymers. Inspired by the stable interactions between metal ions and proteins, high external surface iron-nickel double hydroxides (Fe–Ni LDH) derived from metal–organic framework were selected as carriers to develop high-performance surface bovine serum albumin (BSA) imprinted iron-nickel double hydroxides nanorods (Fe–Ni LDH@MIP). A hexagonal hollow structure Fe–Ni LDH was synthesized with nanosheets stacked on the surface by etching MIL-88A with Ni
2+
. The etching of Ni
2+
increased the surface roughness of MIL-88A and the rough surface of the carrier was conducive to improving the anchorage amount of BSA, thus providing more effective imprinting sites. Controlled coating of the imprinted polymer layer on the surface of Fe–Ni LDH was obtained by aqueous phase precipitation polymerization. The protein adsorption amount reached 329.8 ± 7.8 mg/g in 60 min with an imprinting factor of 2.86. Fe–Ni LDH@MIP also demonstrated excellent and specific recognition ability in the separation of mixed proteins and fetal bovine serum (FBS) and had good adsorption selectivity, whose adsorption capacity only decreased by 11.5% after 7 adsorption–desorption cycles. In short, Fe–Ni LDH@MIP has great potential to apply in the separation and purification of biomolecules.
Graphical abstract |
doi_str_mv | 10.1007/s10853-024-10382-4 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_3126241486</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3126241486</sourcerecordid><originalsourceid>FETCH-LOGICAL-c200t-74ba9c1f9c48136952f8bc10d9b1f8862966fdbbeb2b289943c8d308020a6bd53</originalsourceid><addsrcrecordid>eNp9kLtOwzAUhi0EEqXwAkyWmAPHlyTOiCoKlSpYYGKwfEvjqo2LnQLdeAfekCchJUhsTGf5v_-c8yF0TuCSAJRXiYDIWQaUZwSYoBk_QCOSlyzjAtghGgFQmlFekGN0ktISAPKSkhF6nq030beds3jqvj4-7z22YatXDjc7G8O7tw63qg0x2ITffNfgxi8anNzKmc6_OryJoXO-xcqmEDedDy02aqOM73an6KhWq-TOfucYPU1vHid32fzhdja5nmeGAnRZybWqDKkrwwVhRZXTWmhDwFaa1EIUtCqK2mrtNNVUVBVnRlgGAiioQtucjdHF0Nvf8rJ1qZPLsI1tv1IyQgvKCRdFn6JDysSQUnS17B9fq7iTBOReohwkyl6i_JEoeQ-xAUp7SwsX_6r_ob4Bkv12Tg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>3126241486</pqid></control><display><type>article</type><title>Imprinted Fe–Ni double hydroxide nanorods with high selective protein adsorption capacity</title><source>Springer Nature</source><creator>Wang, Ting ; Lyu, Yanting ; Zhao, Kehan ; Ahmad, Mudasir ; Zhang, Baoliang</creator><creatorcontrib>Wang, Ting ; Lyu, Yanting ; Zhao, Kehan ; Ahmad, Mudasir ; Zhang, Baoliang</creatorcontrib><description>Anchoring more template proteins on the carrier surface is one of the most critical steps in the preparation process of protein-imprinted polymers. Inspired by the stable interactions between metal ions and proteins, high external surface iron-nickel double hydroxides (Fe–Ni LDH) derived from metal–organic framework were selected as carriers to develop high-performance surface bovine serum albumin (BSA) imprinted iron-nickel double hydroxides nanorods (Fe–Ni LDH@MIP). A hexagonal hollow structure Fe–Ni LDH was synthesized with nanosheets stacked on the surface by etching MIL-88A with Ni
2+
. The etching of Ni
2+
increased the surface roughness of MIL-88A and the rough surface of the carrier was conducive to improving the anchorage amount of BSA, thus providing more effective imprinting sites. Controlled coating of the imprinted polymer layer on the surface of Fe–Ni LDH was obtained by aqueous phase precipitation polymerization. The protein adsorption amount reached 329.8 ± 7.8 mg/g in 60 min with an imprinting factor of 2.86. Fe–Ni LDH@MIP also demonstrated excellent and specific recognition ability in the separation of mixed proteins and fetal bovine serum (FBS) and had good adsorption selectivity, whose adsorption capacity only decreased by 11.5% after 7 adsorption–desorption cycles. In short, Fe–Ni LDH@MIP has great potential to apply in the separation and purification of biomolecules.
Graphical abstract</description><identifier>ISSN: 0022-2461</identifier><identifier>EISSN: 1573-4803</identifier><identifier>DOI: 10.1007/s10853-024-10382-4</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Adsorption ; Biomolecules ; Cattle ; Characterization and Evaluation of Materials ; Chemical Routes to Materials ; Chemistry and Materials Science ; Classical Mechanics ; Crystallography and Scattering Methods ; Etching ; Hydroxides ; Imprinted polymers ; Iron ; Materials Science ; Metal-organic frameworks ; Nanorods ; Nickel ; Polymer Sciences ; Protein adsorption ; Proteins ; Separation ; Serum albumin ; Solid Mechanics ; Surface roughness</subject><ispartof>Journal of materials science, 2024-11, Vol.59 (42), p.19837-19854</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c200t-74ba9c1f9c48136952f8bc10d9b1f8862966fdbbeb2b289943c8d308020a6bd53</cites><orcidid>0000-0002-0290-4949</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids></links><search><creatorcontrib>Wang, Ting</creatorcontrib><creatorcontrib>Lyu, Yanting</creatorcontrib><creatorcontrib>Zhao, Kehan</creatorcontrib><creatorcontrib>Ahmad, Mudasir</creatorcontrib><creatorcontrib>Zhang, Baoliang</creatorcontrib><title>Imprinted Fe–Ni double hydroxide nanorods with high selective protein adsorption capacity</title><title>Journal of materials science</title><addtitle>J Mater Sci</addtitle><description>Anchoring more template proteins on the carrier surface is one of the most critical steps in the preparation process of protein-imprinted polymers. Inspired by the stable interactions between metal ions and proteins, high external surface iron-nickel double hydroxides (Fe–Ni LDH) derived from metal–organic framework were selected as carriers to develop high-performance surface bovine serum albumin (BSA) imprinted iron-nickel double hydroxides nanorods (Fe–Ni LDH@MIP). A hexagonal hollow structure Fe–Ni LDH was synthesized with nanosheets stacked on the surface by etching MIL-88A with Ni
2+
. The etching of Ni
2+
increased the surface roughness of MIL-88A and the rough surface of the carrier was conducive to improving the anchorage amount of BSA, thus providing more effective imprinting sites. Controlled coating of the imprinted polymer layer on the surface of Fe–Ni LDH was obtained by aqueous phase precipitation polymerization. The protein adsorption amount reached 329.8 ± 7.8 mg/g in 60 min with an imprinting factor of 2.86. Fe–Ni LDH@MIP also demonstrated excellent and specific recognition ability in the separation of mixed proteins and fetal bovine serum (FBS) and had good adsorption selectivity, whose adsorption capacity only decreased by 11.5% after 7 adsorption–desorption cycles. In short, Fe–Ni LDH@MIP has great potential to apply in the separation and purification of biomolecules.
Graphical abstract</description><subject>Adsorption</subject><subject>Biomolecules</subject><subject>Cattle</subject><subject>Characterization and Evaluation of Materials</subject><subject>Chemical Routes to Materials</subject><subject>Chemistry and Materials Science</subject><subject>Classical Mechanics</subject><subject>Crystallography and Scattering Methods</subject><subject>Etching</subject><subject>Hydroxides</subject><subject>Imprinted polymers</subject><subject>Iron</subject><subject>Materials Science</subject><subject>Metal-organic frameworks</subject><subject>Nanorods</subject><subject>Nickel</subject><subject>Polymer Sciences</subject><subject>Protein adsorption</subject><subject>Proteins</subject><subject>Separation</subject><subject>Serum albumin</subject><subject>Solid Mechanics</subject><subject>Surface roughness</subject><issn>0022-2461</issn><issn>1573-4803</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNp9kLtOwzAUhi0EEqXwAkyWmAPHlyTOiCoKlSpYYGKwfEvjqo2LnQLdeAfekCchJUhsTGf5v_-c8yF0TuCSAJRXiYDIWQaUZwSYoBk_QCOSlyzjAtghGgFQmlFekGN0ktISAPKSkhF6nq030beds3jqvj4-7z22YatXDjc7G8O7tw63qg0x2ITffNfgxi8anNzKmc6_OryJoXO-xcqmEDedDy02aqOM73an6KhWq-TOfucYPU1vHid32fzhdja5nmeGAnRZybWqDKkrwwVhRZXTWmhDwFaa1EIUtCqK2mrtNNVUVBVnRlgGAiioQtucjdHF0Nvf8rJ1qZPLsI1tv1IyQgvKCRdFn6JDysSQUnS17B9fq7iTBOReohwkyl6i_JEoeQ-xAUp7SwsX_6r_ob4Bkv12Tg</recordid><startdate>20241101</startdate><enddate>20241101</enddate><creator>Wang, Ting</creator><creator>Lyu, Yanting</creator><creator>Zhao, Kehan</creator><creator>Ahmad, Mudasir</creator><creator>Zhang, Baoliang</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0002-0290-4949</orcidid></search><sort><creationdate>20241101</creationdate><title>Imprinted Fe–Ni double hydroxide nanorods with high selective protein adsorption capacity</title><author>Wang, Ting ; Lyu, Yanting ; Zhao, Kehan ; Ahmad, Mudasir ; Zhang, Baoliang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c200t-74ba9c1f9c48136952f8bc10d9b1f8862966fdbbeb2b289943c8d308020a6bd53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Adsorption</topic><topic>Biomolecules</topic><topic>Cattle</topic><topic>Characterization and Evaluation of Materials</topic><topic>Chemical Routes to Materials</topic><topic>Chemistry and Materials Science</topic><topic>Classical Mechanics</topic><topic>Crystallography and Scattering Methods</topic><topic>Etching</topic><topic>Hydroxides</topic><topic>Imprinted polymers</topic><topic>Iron</topic><topic>Materials Science</topic><topic>Metal-organic frameworks</topic><topic>Nanorods</topic><topic>Nickel</topic><topic>Polymer Sciences</topic><topic>Protein adsorption</topic><topic>Proteins</topic><topic>Separation</topic><topic>Serum albumin</topic><topic>Solid Mechanics</topic><topic>Surface roughness</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Ting</creatorcontrib><creatorcontrib>Lyu, Yanting</creatorcontrib><creatorcontrib>Zhao, Kehan</creatorcontrib><creatorcontrib>Ahmad, Mudasir</creatorcontrib><creatorcontrib>Zhang, Baoliang</creatorcontrib><collection>CrossRef</collection><jtitle>Journal of materials science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Ting</au><au>Lyu, Yanting</au><au>Zhao, Kehan</au><au>Ahmad, Mudasir</au><au>Zhang, Baoliang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Imprinted Fe–Ni double hydroxide nanorods with high selective protein adsorption capacity</atitle><jtitle>Journal of materials science</jtitle><stitle>J Mater Sci</stitle><date>2024-11-01</date><risdate>2024</risdate><volume>59</volume><issue>42</issue><spage>19837</spage><epage>19854</epage><pages>19837-19854</pages><issn>0022-2461</issn><eissn>1573-4803</eissn><abstract>Anchoring more template proteins on the carrier surface is one of the most critical steps in the preparation process of protein-imprinted polymers. Inspired by the stable interactions between metal ions and proteins, high external surface iron-nickel double hydroxides (Fe–Ni LDH) derived from metal–organic framework were selected as carriers to develop high-performance surface bovine serum albumin (BSA) imprinted iron-nickel double hydroxides nanorods (Fe–Ni LDH@MIP). A hexagonal hollow structure Fe–Ni LDH was synthesized with nanosheets stacked on the surface by etching MIL-88A with Ni
2+
. The etching of Ni
2+
increased the surface roughness of MIL-88A and the rough surface of the carrier was conducive to improving the anchorage amount of BSA, thus providing more effective imprinting sites. Controlled coating of the imprinted polymer layer on the surface of Fe–Ni LDH was obtained by aqueous phase precipitation polymerization. The protein adsorption amount reached 329.8 ± 7.8 mg/g in 60 min with an imprinting factor of 2.86. Fe–Ni LDH@MIP also demonstrated excellent and specific recognition ability in the separation of mixed proteins and fetal bovine serum (FBS) and had good adsorption selectivity, whose adsorption capacity only decreased by 11.5% after 7 adsorption–desorption cycles. In short, Fe–Ni LDH@MIP has great potential to apply in the separation and purification of biomolecules.
Graphical abstract</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s10853-024-10382-4</doi><tpages>18</tpages><orcidid>https://orcid.org/0000-0002-0290-4949</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0022-2461 |
ispartof | Journal of materials science, 2024-11, Vol.59 (42), p.19837-19854 |
issn | 0022-2461 1573-4803 |
language | eng |
recordid | cdi_proquest_journals_3126241486 |
source | Springer Nature |
subjects | Adsorption Biomolecules Cattle Characterization and Evaluation of Materials Chemical Routes to Materials Chemistry and Materials Science Classical Mechanics Crystallography and Scattering Methods Etching Hydroxides Imprinted polymers Iron Materials Science Metal-organic frameworks Nanorods Nickel Polymer Sciences Protein adsorption Proteins Separation Serum albumin Solid Mechanics Surface roughness |
title | Imprinted Fe–Ni double hydroxide nanorods with high selective protein adsorption capacity |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T00%3A30%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Imprinted%20Fe%E2%80%93Ni%20double%20hydroxide%20nanorods%20with%20high%20selective%20protein%20adsorption%20capacity&rft.jtitle=Journal%20of%20materials%20science&rft.au=Wang,%20Ting&rft.date=2024-11-01&rft.volume=59&rft.issue=42&rft.spage=19837&rft.epage=19854&rft.pages=19837-19854&rft.issn=0022-2461&rft.eissn=1573-4803&rft_id=info:doi/10.1007/s10853-024-10382-4&rft_dat=%3Cproquest_cross%3E3126241486%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c200t-74ba9c1f9c48136952f8bc10d9b1f8862966fdbbeb2b289943c8d308020a6bd53%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=3126241486&rft_id=info:pmid/&rfr_iscdi=true |