Ring -opening of polythiolactones to construct protein-imprinted nanospheres with high recognition and regulation capabilities. Issue 45 (25th October 2022)
- Record Type:
- Journal Article
- Title:
- Ring -opening of polythiolactones to construct protein-imprinted nanospheres with high recognition and regulation capabilities. Issue 45 (25th October 2022)
- Main Title:
- Ring -opening of polythiolactones to construct protein-imprinted nanospheres with high recognition and regulation capabilities
- Authors:
- Wang, Mingqi
Zhang, Guoxian
Liu, Qing
Wei, Mengmeng
Ren, Yafeng
Fa, Shixin
Zhang, Qiuyu - Abstract:
- Abstract : This work proposes a novel protein imprinted strategy by crosslinking multifunctionlized polythiolactone nanospheres. The prepared protein imprinted magnetic nanospheres show tunable rebinding capacity and specificity for bovine serum albumin. Abstract : Developing and preparing novel protein-imprinted nanomaterials with high recognition ability remains challenging because it is difficult to controllably and orderly design and arrange functional groups on the imprinted polymer layers of protein-imprinted nanomaterials to improve their protein identification. Herein, we present a new technology using rationally designed polythiolactone-decorated magnetic nanospheres as the precursor of multifunctionalized imprinted materials. Moreover, the strategy of ring-opening the polythiolactione layers using primary amines with terminal alcohols, acids and pyrrolidines introduces abundant recognition sites, which enhance the recognition for template proteins through multiple hydrogen-bonding and hydrophobic interactions. Thiols generated in situ by the ring-opening reaction provide sufficient crosslinking sites proximate to each recognition site for the formation of imprinting cavities, endowing the imprinted nanospheres with promising regulation capabilities. Based on the rational design, the imprinted nanospheres can be prepared conveniently and present tunable rebinding capacity and specificity for bovine serum albumin (BSA). The maximum saturated rebinding capacity ofAbstract : This work proposes a novel protein imprinted strategy by crosslinking multifunctionlized polythiolactone nanospheres. The prepared protein imprinted magnetic nanospheres show tunable rebinding capacity and specificity for bovine serum albumin. Abstract : Developing and preparing novel protein-imprinted nanomaterials with high recognition ability remains challenging because it is difficult to controllably and orderly design and arrange functional groups on the imprinted polymer layers of protein-imprinted nanomaterials to improve their protein identification. Herein, we present a new technology using rationally designed polythiolactone-decorated magnetic nanospheres as the precursor of multifunctionalized imprinted materials. Moreover, the strategy of ring-opening the polythiolactione layers using primary amines with terminal alcohols, acids and pyrrolidines introduces abundant recognition sites, which enhance the recognition for template proteins through multiple hydrogen-bonding and hydrophobic interactions. Thiols generated in situ by the ring-opening reaction provide sufficient crosslinking sites proximate to each recognition site for the formation of imprinting cavities, endowing the imprinted nanospheres with promising regulation capabilities. Based on the rational design, the imprinted nanospheres can be prepared conveniently and present tunable rebinding capacity and specificity for bovine serum albumin (BSA). The maximum saturated rebinding capacity of imprinted materials for BSA is up to 285 ± 15 mg g −1 and the highest imprinting factor reaches 5.79. The simple and versatile strategy demonstrated in this study shows promise for the design of other protein-imprinted materials with high recognition ability. … (more)
- Is Part Of:
- Nanoscale. Volume 14:Issue 45(2022)
- Journal:
- Nanoscale
- Issue:
- Volume 14:Issue 45(2022)
- Issue Display:
- Volume 14, Issue 45 (2022)
- Year:
- 2022
- Volume:
- 14
- Issue:
- 45
- Issue Sort Value:
- 2022-0014-0045-0000
- Page Start:
- 16865
- Page End:
- 16873
- Publication Date:
- 2022-10-25
- Subjects:
- Nanoscience -- Periodicals
Nanotechnology -- Periodicals
620.505 - Journal URLs:
- http://www.rsc.org/Publishing/Journals/NR/Index.asp ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d2nr03715g ↗
- Languages:
- English
- ISSNs:
- 2040-3364
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 9830.266000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 24430.xml