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- W4288428503 abstract "Abstract The capacity to precisely modulate aptamer affinity is important for a wide variety of applications. However, most such engineering strategies entail laborious trial-and-error testing or require prior knowledge of an aptamer’s structure and ligand-binding domain. We describe here a simple and generalizable strategy for allosteric modulation of aptamer affinity by employing a double-stranded molecular clamp that destabilizes aptamer secondary structure through mechanical tension. We demonstrate the effectiveness of the approach with a thrombin-binding aptamer and show that we can alter its affinity by as much as 65-fold. We also show that this modulation can be rendered reversible by introducing a restriction enzyme cleavage site into the molecular clamp domain and describe a design strategy for achieving even more finely-tuned affinity modulation. This strategy requires no prior knowledge of the aptamer’s structure and binding mechanism and should thus be generalizable across aptamers." @default.
- W4288428503 created "2022-07-29" @default.
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- W4288428503 date "2022-07-28" @default.
- W4288428503 modified "2023-09-29" @default.
- W4288428503 title "Allosteric Regulation of Aptamer Affinity through Mechano-Chemical Coupling" @default.
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- W4288428503 doi "https://doi.org/10.1101/2022.07.28.501929" @default.
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