Table 2 Thermodynamic parameters and binding affinities of wild-type LP and mutant M15 aptamer with the natural ligand FMN and synthetic ligands DHEF, MHEF, and FMFa

From: Rational development of FMN-based orthogonal riboswitch that functions in response to specific non-cognate ligand

Aptamer

Ligand

−ΔH° bind

−TΔS° bind

−ΔG° 25 bind

KD

  

[kcal mol−1]

[kcal mol−1]

[kcal mol−1]

[× 10−6 L mol−1]

LP

FMN

12.8 ± 0.92

2.80 ± 1.03

9.95 ± 0.11

0.051 ± 0.007

DHEF

 

NB

  

MHEF

 

NB

  

FMF

 

NB

  

M15

FMN

 

NB

  

DHEF

16.7 ± 0.57

7.00 ± 0.61

9.70 ± 0.04

0.075 ± 0.01

MHEF

5.05 ± 0.45

7.28 ± 3.83

7.60 ± 3.28

0.054 ± 0.005

FMF

12.1 ± 1.84

2.29 ± 2.12

9.85 ± 0.36

0.068 ± 0.004

  1. Data are shown as mean ± standard deviation (SD).
  2. NB no binding.
  3. aITC Data was acquired at 25 °C in a buffer containing 50 mM MOPS (pH 7.5), 100 mM NaCl, 2 mM MgCl2, and 1% DMSO.
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