Table 1 Thermodynamic parameters for the KIX binding of Myb32 mutants.

From: Rational design of a helical peptide inhibitor targeting c-Myb–KIX interaction

Myb32

Kd (μM)

N

ΔH (kcal mol–1)

TΔS (kcal mol–1)

ΔG (kcal mol–1)

WT

0.22 ± 0.01

0.97 ± 0.01

–6.49 ± 0.05

–2.74 ± 0.04

–9.23 ± 0.04

K291R

0.21 ± 0.01

0.97 ± 0.01

–6.46 ± 0.04

–2.80 ± 0.01

–9.27 ± 0.04

E292L

0.48 ± 0.03

0.92 ± 0.02

–5.45 ± 0.03

–3.32 ± 0.01

–8.77 ± 0.04

K293R

0.22 ± 0.01

0.94 ± 0.01

–7.03 ± 0.01

–2.21 ± 0.02

–9.23 ± 0.01

K296R

0.16 ± 0.01

0.96 ± 0.02

–6.3 ± 0.1

–3.2 ± 0.2

–9.44 ± 0.04

K291R/K293R

0.14 ± 0.01

0.84 ± 0.02

–7.31 ± 0.04

–2.21 ± 0.03

–9.51 ± 0.01

K291R/K296R

0.12 ± 0.01

0.90 ± 0.01

–7.56 ± 0.03

–2.05 ± 0.03

–9.62 ± 0.05

K293R/K296R

0.13 ± 0.01

0.96 ± 0.01

–7.31 ± 0.04

–2.23 ± 0.08

–9.54 ± 0.04

RRR

0.08 ± 0.01

0.99 ± 0.01

–7.57 ± 0.03

–2.27 ± 0.07

–9.84 ± 0.09

WT (SPR)a

0.51 ± 0.02

0.99 ± 0.02

–13.79 ± 0.03

5.07 ± 0.05

–8.72 ± 0.02

RRR (SPR)

0.26 ± 0.01

0.99 ± 0.01

–14.80 ± 0.03

5.67 ± 0.02

–9.14 ± 0.01

  1. The dissociation constant (Kd), stoichiometry of binding (N), and changes in enthalpy (ΔH), entropy (ΔS), and Gibbs free energy (ΔG) upon binding were obtained by ITC measurements (20 mM Tris-acetate [pH 7.0] and 50 mM NaCl). T is the temperature. All measurements were performed more than twice, and the means and standard errors are shown.
  2. aThe ITC measurement was performed under the conditions for SPR measurement (20 mM sodium phosphate [pH 7.0] and 300 mM NaCl).