Literature DB >> 31912723

Designed Alteration of Binding Affinity in Structure-Switching Aptamers through the Use of Dangling Nucleotides.

Sladjana Slavkovic1, Sophie R Eisen1, Philip E Johnson1.   

Abstract

The ability to change binding affinity in a controlled fashion is a key step in the rational design of biomolecules in general and functional nucleic acids in particular. Here, we use dangling nucleotides to alter the binding affinity of structure-switching aptamers. Dangling nucleotides can stabilize or destabilize a nucleic acid structure with a known ΔG°37. When the dangling nucleotide stabilizes the structure, less free energy from ligand binding is needed to fold the molecule and hence the ligand is observed to bind tighter than in the absence of the unpaired nucleotide. For a destabilizing dangling nucleotide, the opposite occurs, and the observed binding is weaker. We demonstrate this concept using both the cocaine-binding aptamer and the ATP-binding aptamer systems. We find that for both aptamers there is a direct, but different, relationship between the predicted stabilization and the change in the observed binding free energy.

Entities:  

Year:  2020        PMID: 31912723     DOI: 10.1021/acs.biochem.9b00630

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  2 in total

1.  Reduction in Dynamics of Base pair Opening upon Ligand Binding by the Cocaine-Binding Aptamer.

Authors:  Zachary R Churcher; Devid Garaev; Howard N Hunter; Philip E Johnson
Journal:  Biophys J       Date:  2020-08-15       Impact factor: 4.033

2.  Thermodynamic analysis of cooperative ligand binding by the ATP-binding DNA aptamer indicates a population-shift binding mechanism.

Authors:  Sladjana Slavkovic; Yanrui Zhu; Zachary R Churcher; Aron A Shoara; Anne E Johnson; Philip E Johnson
Journal:  Sci Rep       Date:  2020-11-03       Impact factor: 4.379

  2 in total

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