DNA–Nanoparticle Composites Synergistically Enhance Organophosphate Hydrolase Enzymatic Activity
Source abstract
Abstract
Cell-free synthetic biology relies on optimally exploiting enzymatic activity, and recent demonstrations that nanoparticle (NP) and DNA scaffolding can enhance enzyme activity suggest new avenues toward this. A modular architecture consisting of a DNA cage displaying semiconductor quantum dots (QDs) that, in turn, ratiometrically display the organophosphate hydrolase phosphotriesterase (PTE) was utilized as a model system. Increasing DNA cage concentration relative to QD-PTE and creating a dense composite enhanced PTE rates up to 12.5-fold, suggesting strong synergy between the NP and DNA components; this putatively arises from increased enzymatic stability and alleviation of its rate-limiting step. Such bioinorganic composites may offer new scaffolding approaches for synthetic biology.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · DNA and Nucleic Acid Chemistry · RNA Interference and Gene Delivery
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
College of Science, George Mason University, Fairfax, Virginia 22030, United States
KeyW Corporation, Hanover, Maryland 21076, United States
Funding
U.S. Naval Research Laboratory · Office of Naval Research · U.S. Department of Agriculture
References (31)
Show source-provided references
1. 10.1016/j.cell.2014.02.03910.1016/j.cell.2014.02.039 ↗
2. 10.1038/nrg277510.1038/nrg2775 ↗
3. 10.1016/j.cell.2016.09.01310.1016/j.cell.2016.09.013 ↗
4. 10.1021/acssynbio.5b0029610.1021/acssynbio.5b00296 ↗
5. 10.1038/nchembio.206210.1038/nchembio.2062 ↗
6. 10.1016/j.nantod.2014.02.00510.1016/j.nantod.2014.02.005 ↗
7. 10.1016/j.copbio.2015.04.00510.1016/j.copbio.2015.04.005 ↗
8. 10.1098/rsif.2013.093110.1098/rsif.2013.0931 ↗
9. 10.1021/acsnano.5b0345910.1021/acsnano.5b03459 ↗
10. 10.1039/C7NH00052A10.1039/C7NH00052A ↗
11. 10.1038/ncomms1061910.1038/ncomms10619 ↗
12. 10.1038/nprot.2016.13910.1038/nprot.2016.139 ↗
13. 10.1002/anie.20170380610.1002/anie.201703806 ↗
14. 10.1088/2399-1984/aa656110.1088/2399-1984/aa6561 ↗
15. 10.1021/acs.chemmater.7b0010810.1021/acs.chemmater.7b00108 ↗
16. 10.1016/j.ccr.2013.08.03010.1016/j.ccr.2013.08.030 ↗
17. 10.1002/adfm.20170029010.1002/adfm.201700290 ↗
18. 10.1021/bi300811t10.1021/bi300811t ↗
19. 10.1021/acs.langmuir.7b0258810.1021/acs.langmuir.7b02588 ↗
20. 10.1039/C6AN02575G10.1039/C6AN02575G ↗
21. 10.1016/S0926-6593(65)80190-410.1016/S0926-6593(65)80190-4 ↗
22. Cornish-Bowden A. · 2013
23. 10.1021/acsnano.7b0162410.1021/acsnano.7b01624 ↗
24. 10.1126/science.126141210.1126/science.1261412 ↗
25. 10.1002/anie.20170380610.1002/anie.201703806 ↗
26. 10.1038/ncomms1398210.1038/ncomms13982 ↗
27. 10.1021/ac200853a10.1021/ac200853a ↗
28. 10.1021/jp511046710.1021/jp5110467 ↗
29. 10.1039/C5RA21187E10.1039/C5RA21187E ↗
30. 10.1021/acsami.8b0271710.1021/acsami.8b02717 ↗
31. 10.1039/C7NR00200A10.1039/C7NR00200A ↗