Journal
ACS NANO
Volume 14, Issue 7, Pages 8776-8783Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.0c03362
Keywords
DNA framework; molecular confinement; thermodynamic stability; aptamer; biomimicry
Categories
Funding
- National Key R&D Program of China [2018YFA0902600]
- National Natural Science Foundation of China [21804088, 21904086, 21804091, 21904041, 21834007]
- China Postdoctoral Science Foundation [2019M661417]
- Shanghai Municipal Education Commission-Gaofeng Clinical Medicine Grant Support [20171913]
- Shuguang Program - Shanghai Education Development Foundation [18SG16]
- Shanghai Municipal Education Commission [18SG16]
- Innovative Research Team of High Level Local Universities in Shanghai [SSMUZLCX20180701]
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Active sites of proteins are generally encapsulated within three-dimensional peptide scaffolds that provide the molecular-scale confinement microenvironment. Nevertheless, the ability to tune thermodynamic stability in biomimetic molecular confinement relies on the macromolecular crowding effect of lack of stoichiometry and reconfigurability. Here, we report a framework nucleic acid (FNA)-based strategy to increase thermodynamic stability of aptamers. We demonstrate that the molecular-scale confinement increases the thermodynamic stability of aptamers via facilitated folding kinetics, which is confirmed by the single-molecule FRET (smFRET). Unfavorable conformations of aptamers are restricted as revealed by the Monte Carlo simulation. The binding affinity of the DNA framework-confined aptamer is improved by similar to 3-fold. With a similar strategy we improve the catalytic activity of heminbinding aptamer. Our approach thus shows high potential for designing protein-mimicking DNA nanostructures with enhanced binding affinity and catalytic activity for biosensing and biomedical engineering.
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