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. Author manuscript; available in PMC: 2014 Feb 1.
Published in final edited form as: ChemMedChem. 2012 Dec 13;8(2):10.1002/cmdc.201200422. doi: 10.1002/cmdc.201200422

Table 2.

Thermodynamic values for the binding of UM-24, KR-41 and KR-42 to gp120.

Peptide ITC[b] (KD, nM) ΔG (kcalmol−1) ΔH (kcalmol−1) −TΔS (kcalmol−1)
UM-24 21.1 ±1.4 −10.5±0.8 −14.1±0.6 +3.6±1.6
KR-41 70.0±1.6 −9.8 ±1.7 −14.9±7.5 +5.1±2.6
KR-42 282.1±2.2 −8.9 ±2.9 −14.6±1.7 +5.7±2.2
[b]

Data collected in duplicate. ITC experiments were performed at 25°C in 1xPBS (pH 7.4). The dissociation constant (Kd) and the change in enthalpy (ΔH) were determined at 25°C by isothermal titration calorimetry using a VP-ITC titration calorimetric system from MicoCal/GE Healthcare (Northampton, MA, USA). ΔG and −TΔS were calculated using the equations: ΔG = −RTln(1/Kd), ΔG = ΔH − TΔS. The data are reported as the mean with standard deviation.