Functionalized Nano-adsorbent for Affinity Separation of Proteins
Abstract Thiol-functionalized silica nanospheres (SiO2-SH NSs) with an average diameter of 460 nm were synthesized through a hydrothermal route. Subsequently, the prepared SiO2-SH NSs were modified by SnO2 quantum dots to afford SnO2/SiO2 composite NSs possessing obvious fluorescence, which could be...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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SpringerOpen
2018-05-01
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| Series: | Nanoscale Research Letters |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1186/s11671-018-2531-4 |
| _version_ | 1827833872099835904 |
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| author | Xueyan Zou Fengbo Yang Xin Sun Mingming Qin Yanbao Zhao Zhijun Zhang |
| author_facet | Xueyan Zou Fengbo Yang Xin Sun Mingming Qin Yanbao Zhao Zhijun Zhang |
| author_sort | Xueyan Zou |
| collection | DOAJ |
| description | Abstract Thiol-functionalized silica nanospheres (SiO2-SH NSs) with an average diameter of 460 nm were synthesized through a hydrothermal route. Subsequently, the prepared SiO2-SH NSs were modified by SnO2 quantum dots to afford SnO2/SiO2 composite NSs possessing obvious fluorescence, which could be used to trace the target protein. The SnO2/SiO2 NSs were further modified by reduced glutathione (GSH) to obtain SnO2/SiO2-GSH NSs, which can specifically separate glutathione S-transferase-tagged (GST-tagged) protein. Moreover, the peroxidase activity of glutathione peroxidase 3 (GPX3) separated from SnO2/SiO2-GSH NSs in vitro was evaluated. Results show that the prepared SnO2/SiO2-GSH NSs exhibit negligible nonspecific adsorption, high concentration of protein binding (7.4 mg/g), and good reused properties. In the meantime, the GST-tagged GPX3 separated by these NSs can retain its redox state and peroxidase activity. Therefore, the prepared SnO2/SiO2-GSH NSs might find promising application in the rapid separation and purification of GST-tagged proteins. |
| first_indexed | 2024-03-12T05:40:41Z |
| format | Article |
| id | doaj.art-94dca64fd15345b0a0e9b4e683efce6e |
| institution | Directory Open Access Journal |
| issn | 1931-7573 1556-276X |
| language | English |
| last_indexed | 2024-03-12T05:40:41Z |
| publishDate | 2018-05-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | Nanoscale Research Letters |
| spelling | doaj.art-94dca64fd15345b0a0e9b4e683efce6e2023-09-03T06:09:07ZengSpringerOpenNanoscale Research Letters1931-75731556-276X2018-05-011311810.1186/s11671-018-2531-4Functionalized Nano-adsorbent for Affinity Separation of ProteinsXueyan Zou0Fengbo Yang1Xin Sun2Mingming Qin3Yanbao Zhao4Zhijun Zhang5Engineering Research Center for Nanomaterials, Henan UniversityInstitute of Plant Stress Biology-State Key Laboratory of Cotton Biology, Henan UniversityEngineering Research Center for Nanomaterials, Henan UniversityEngineering Research Center for Nanomaterials, Henan UniversityEngineering Research Center for Nanomaterials, Henan UniversityEngineering Research Center for Nanomaterials, Henan UniversityAbstract Thiol-functionalized silica nanospheres (SiO2-SH NSs) with an average diameter of 460 nm were synthesized through a hydrothermal route. Subsequently, the prepared SiO2-SH NSs were modified by SnO2 quantum dots to afford SnO2/SiO2 composite NSs possessing obvious fluorescence, which could be used to trace the target protein. The SnO2/SiO2 NSs were further modified by reduced glutathione (GSH) to obtain SnO2/SiO2-GSH NSs, which can specifically separate glutathione S-transferase-tagged (GST-tagged) protein. Moreover, the peroxidase activity of glutathione peroxidase 3 (GPX3) separated from SnO2/SiO2-GSH NSs in vitro was evaluated. Results show that the prepared SnO2/SiO2-GSH NSs exhibit negligible nonspecific adsorption, high concentration of protein binding (7.4 mg/g), and good reused properties. In the meantime, the GST-tagged GPX3 separated by these NSs can retain its redox state and peroxidase activity. Therefore, the prepared SnO2/SiO2-GSH NSs might find promising application in the rapid separation and purification of GST-tagged proteins.http://link.springer.com/article/10.1186/s11671-018-2531-4Silica nanospheresSnO2Affinity separationPeroxidase activityRedox state |
| spellingShingle | Xueyan Zou Fengbo Yang Xin Sun Mingming Qin Yanbao Zhao Zhijun Zhang Functionalized Nano-adsorbent for Affinity Separation of Proteins Nanoscale Research Letters Silica nanospheres SnO2 Affinity separation Peroxidase activity Redox state |
| title | Functionalized Nano-adsorbent for Affinity Separation of Proteins |
| title_full | Functionalized Nano-adsorbent for Affinity Separation of Proteins |
| title_fullStr | Functionalized Nano-adsorbent for Affinity Separation of Proteins |
| title_full_unstemmed | Functionalized Nano-adsorbent for Affinity Separation of Proteins |
| title_short | Functionalized Nano-adsorbent for Affinity Separation of Proteins |
| title_sort | functionalized nano adsorbent for affinity separation of proteins |
| topic | Silica nanospheres SnO2 Affinity separation Peroxidase activity Redox state |
| url | http://link.springer.com/article/10.1186/s11671-018-2531-4 |
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