journal article·2025-09

A Reverse Transcription Polymerase Chain Reaction‐Based Method for Determining Aptamer–Protein Interactions at Nanoparticle Surfaces

Saketh Gudipati, Shraddha S. Sawant, Rachelle C. Canete, Patrick M. Corrigan, Jessica L. Rouge

ChemNanoMat· Volume 11· Issue 9
Publisher page

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.
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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 ↗