Cargando…
Fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation
Surface immobilization provides a useful platform for biosensing, drug screening, tissue engineering and other chemical and biological applications. However, some of the used reactions are inefficient and/or complicated, limiting their applications in immobilization. Herein, we use a spontaneous and...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8152777/ https://www.ncbi.nlm.nih.gov/pubmed/34122863 http://dx.doi.org/10.1039/d0sc00062k |
_version_ | 1783698667572559872 |
---|---|
author | Zhang, Yiru Shen, Jianlei Hu, Rong Shi, Xiujuan Hu, Xianglong He, Benzhao Qin, Anjun Tang, Ben Zhong |
author_facet | Zhang, Yiru Shen, Jianlei Hu, Rong Shi, Xiujuan Hu, Xianglong He, Benzhao Qin, Anjun Tang, Ben Zhong |
author_sort | Zhang, Yiru |
collection | PubMed |
description | Surface immobilization provides a useful platform for biosensing, drug screening, tissue engineering and other chemical and biological applications. However, some of the used reactions are inefficient and/or complicated, limiting their applications in immobilization. Herein, we use a spontaneous and catalyst-free amino-yne click bioconjugation to generate activated ethynyl group functionalized surfaces for fast immobilization of native proteins and cells. Biomolecules, such as bovine serum albumin (BSA), human IgG and a peptide of C(RGDfK), could be covalently immobilized on the surfaces in as short as 30 min. Notably, the bioactivity of the anchored biomolecules remains intact, which is verified by efficiently capturing target antibodies and cells from the bulk solutions. This strategy represents an alternative for highly efficient surface biofunctionalization. |
format | Online Article Text |
id | pubmed-8152777 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-81527772021-06-11 Fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation Zhang, Yiru Shen, Jianlei Hu, Rong Shi, Xiujuan Hu, Xianglong He, Benzhao Qin, Anjun Tang, Ben Zhong Chem Sci Chemistry Surface immobilization provides a useful platform for biosensing, drug screening, tissue engineering and other chemical and biological applications. However, some of the used reactions are inefficient and/or complicated, limiting their applications in immobilization. Herein, we use a spontaneous and catalyst-free amino-yne click bioconjugation to generate activated ethynyl group functionalized surfaces for fast immobilization of native proteins and cells. Biomolecules, such as bovine serum albumin (BSA), human IgG and a peptide of C(RGDfK), could be covalently immobilized on the surfaces in as short as 30 min. Notably, the bioactivity of the anchored biomolecules remains intact, which is verified by efficiently capturing target antibodies and cells from the bulk solutions. This strategy represents an alternative for highly efficient surface biofunctionalization. The Royal Society of Chemistry 2020-03-18 /pmc/articles/PMC8152777/ /pubmed/34122863 http://dx.doi.org/10.1039/d0sc00062k Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Zhang, Yiru Shen, Jianlei Hu, Rong Shi, Xiujuan Hu, Xianglong He, Benzhao Qin, Anjun Tang, Ben Zhong Fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation |
title | Fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation |
title_full | Fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation |
title_fullStr | Fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation |
title_full_unstemmed | Fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation |
title_short | Fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation |
title_sort | fast surface immobilization of native proteins through catalyst-free amino-yne click bioconjugation |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8152777/ https://www.ncbi.nlm.nih.gov/pubmed/34122863 http://dx.doi.org/10.1039/d0sc00062k |
work_keys_str_mv | AT zhangyiru fastsurfaceimmobilizationofnativeproteinsthroughcatalystfreeaminoyneclickbioconjugation AT shenjianlei fastsurfaceimmobilizationofnativeproteinsthroughcatalystfreeaminoyneclickbioconjugation AT hurong fastsurfaceimmobilizationofnativeproteinsthroughcatalystfreeaminoyneclickbioconjugation AT shixiujuan fastsurfaceimmobilizationofnativeproteinsthroughcatalystfreeaminoyneclickbioconjugation AT huxianglong fastsurfaceimmobilizationofnativeproteinsthroughcatalystfreeaminoyneclickbioconjugation AT hebenzhao fastsurfaceimmobilizationofnativeproteinsthroughcatalystfreeaminoyneclickbioconjugation AT qinanjun fastsurfaceimmobilizationofnativeproteinsthroughcatalystfreeaminoyneclickbioconjugation AT tangbenzhong fastsurfaceimmobilizationofnativeproteinsthroughcatalystfreeaminoyneclickbioconjugation |