A Reverse Transcription Polymerase Chain Reaction‐Based Method for Determining Aptamer–Protein Interactions at Nanoparticle Surfaces
Source abstract
Abstract
Nucleic acid–protein interactions influence the activity and stability of DNA‐ and RNA‐functionalized nanomaterials. Herein, a restriction enzyme‐mediated approach coupled with reverse transcription‐polymerase chain reaction (RT‐PCR) for probing aptamer–protein interactions on a nanoparticle (NP) surface as a general method for identifying interactions between proteins and an RNA on a NP is described. This process is enabled by utilizing a restriction enzyme (RE)‐specific sequence at the NP surface that can be masked and subsequently revealed depending on the bound state of a protein at the particle's surface. The method is suitable for investigating a specific protein interaction versus a nonspecific interaction, using an RT‐PCR assay designed to detect exposed nucleic acid ligands at the NP surface. This approach is highly modular and can be applied to a variety of RNA–protein interactions for bioanalytical purposes, including as a selection pressure for in vitro selections and Systematic Evolution of Ligands by EXponential enrichment protocols.
Source: crossref · Quality: baseline
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · Bacteriophages and microbial interactions · RNA Interference and Gene Delivery
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Chemistry University of Connecticut 55 North Eagleville Road Storrs CT 06269 USA
Funding
University of Connecticut · National Institutes of Health
References (36)
Show source-provided references
1. 10.1126/science.112555910.1126/science.1125559 ↗
2. 10.1021/ac202648w10.1021/ac202648w ↗
3. 10.1021/ac504652e10.1021/ac504652e ↗
4. 10.1021/jacs.5b0067010.1021/jacs.5b00670 ↗
5. 10.1016/j.tibtech.2019.01.00810.1016/j.tibtech.2019.01.008 ↗
6. 10.1073/pnas.151058111210.1073/pnas.1510581112 ↗
7. 10.1038/nnano.2012.23710.1038/nnano.2012.237 ↗
8. 10.2217/nnm.15.18810.2217/nnm.15.188 ↗
9. 10.1016/j.molliq.2018.07.07010.1016/j.molliq.2018.07.070 ↗
10. 10.1021/nn406018q10.1021/nn406018q ↗
11. 10.1007/s12274-018-2191-910.1007/s12274-018-2191-9 ↗
12. 10.1039/C8NR09855G10.1039/C8NR09855G ↗
13. 10.1002/anie.20140921110.1002/anie.201409211 ↗
14. 10.1021/acscentsci.9b0110510.1021/acscentsci.9b01105 ↗
15. 10.1073/pnas.130580411010.1073/pnas.1305804110 ↗
16. 10.1038/s41551-018-0214-110.1038/s41551-018-0214-1 ↗
17. 10.1021/nl051264s10.1021/nl051264s ↗
18. 10.1021/acschembio.7b0043710.1021/acschembio.7b00437 ↗
19. 10.1021/nn503601s10.1021/nn503601s ↗
20. 10.1021/acs.bioconjchem.0c0004710.1021/acs.bioconjchem.0c00047 ↗
21. 10.1021/jacs.5b0710410.1021/jacs.5b07104 ↗
22. 10.1126/science.220012110.1126/science.2200121 ↗
23. 10.1038/346818a010.1038/346818a0 ↗
24. 10.1038/emm.2016.4410.1038/emm.2016.44 ↗
25. 10.3390/ijms2123912310.3390/ijms21239123 ↗
26. 10.1021/acssensors.0c0221210.1021/acssensors.0c02212 ↗
27. 10.1021/jacs.9b1226510.1021/jacs.9b12265 ↗
28. 10.1038/nchem.33410.1038/nchem.334 ↗
29. 10.1021/acs.analchem.0c0356310.1021/acs.analchem.0c03563 ↗
30. 10.1021/acs.analchem.0c0494910.1021/acs.analchem.0c04949 ↗
31. 10.1021/acs.analchem.0c0245510.1021/acs.analchem.0c02455 ↗
32. Narayanan S. · Ann. Clin. Lab. Sci. · 1999 · 29 · 275
33. 10.1006/mthe.2001.049510.1006/mthe.2001.0495 ↗
34. 10.1261/rna.123930810.1261/rna.1239308 ↗
35. 10.1021/ac102114z10.1021/ac102114z ↗
36. 10.1093/nar/gkt95610.1093/nar/gkt956 ↗