Co-immobilization of Enzymes and Aptamers to Create Self-Regenerating Ultrafiltration Membranes for Toxin Removal
Source abstract
Abstract
Aptamer-functionalized membranes are a promising platform for toxin removal and small-molecule sequestration. However, this function can be compromised when the aptamer binding sites become saturated, and regeneration of the membrane requires heat and multiple washes to restore the aptamer binding capabilities. Additionally, bound molecules can be eluted into water sources, resulting in recontamination. Herein, we address this challenge by creating autonomously self-regenerating membranes through the tandem use of aptamers and enzymes to trap and degrade small-molecule contaminants. To demonstrate this approach, we developed an enzyme–aptamer-functionalized membrane that sequesters and degrades the small-molecule contaminant bisphenol A (BPA) from water. We show that BPA is not only depleted but also degraded, as the membrane is able to be reused for multiple cycles without the need for heat or washing to restore function. Given the large number of reported DNA aptamers for small molecule analytes, we envision that this research will provide a broadly applicable platform for the removal of waterborne contaminants.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · Membrane Separation Technologies · Nanopore and Nanochannel Transport Studies
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Chemistry, Emory University, Atlanta, Georgia 30322, United States
Department of Chemistry, Georgia Gwinnett College, Lawrenceville, Georgia 30043, United States
Department of Chemistry, Washington University in St. Louis, St. Louis, Missouri 63130, United States
Funding
Division of Chemical, Bioengineering, Environmental, and Transport Systems
References (25)
Show source-provided references
1. 10.1039/C5EW00159E10.1039/C5EW00159E ↗
2. 10.1002/anie.20160150910.1002/anie.201601509 ↗
3. 10.1016/j.jenvman.2020.11058310.1016/j.jenvman.2020.110583 ↗
4. 10.3390/polym1108125210.3390/polym11081252 ↗
5. 10.1021/acsmaterialslett.9b0028810.1021/acsmaterialslett.9b00288 ↗
6. 10.1021/acs.bioconjchem.1c0034410.1021/acs.bioconjchem.1c00344 ↗
7. 10.1039/D0AN00178C10.1039/D0AN00178C ↗
8. 10.1016/j.memsci.2022.12031310.1016/j.memsci.2022.120313 ↗
9. 10.1016/j.ijbiomac.2017.10.17710.1016/j.ijbiomac.2017.10.177 ↗
10. 10.1016/j.memsci.2014.06.02710.1016/j.memsci.2014.06.027 ↗
11. 10.1021/acs.est.6b0164110.1021/acs.est.6b01641 ↗
12. 10.1016/j.ibiod.2016.03.01710.1016/j.ibiod.2016.03.017 ↗
13. 10.1016/j.jenvman.2022.11467610.1016/j.jenvman.2022.114676 ↗
14. 10.1016/j.biortech.2018.09.12910.1016/j.biortech.2018.09.129 ↗
15. 10.1016/j.cej.2020.12627210.1016/j.cej.2020.126272 ↗
16. 10.1080/01496395.2019.164851110.1080/01496395.2019.1648511 ↗
17. 10.1007/s13205-019-1648-110.1007/s13205-019-1648-1 ↗
18. 10.1007/s00449-017-1783-110.1007/s00449-017-1783-1 ↗
19. 10.1016/j.jcis.2010.05.03110.1016/j.jcis.2010.05.031 ↗
20. 10.1016/j.chemosphere.2021.13175710.1016/j.chemosphere.2021.131757 ↗
21. 10.1021/acsami.7b0237710.1021/acsami.7b02377 ↗
22. 10.1080/07388551.2017.141723410.1080/07388551.2017.1417234 ↗
23. 10.3389/fbioe.2021.77823910.3389/fbioe.2021.778239 ↗
24. 10.1155/2017/371207010.1155/2017/3712070 ↗
25. 10.1039/D2SC00117A10.1039/D2SC00117A ↗