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Fig. 4 | Retrovirology

Fig. 4

From: Altered Env conformational dynamics as a mechanism of resistance to peptide-triazole HIV-1 inactivators

Fig. 4

Thermodynamic dissection of AAR029b and KR13 binding to wild type and resistant gp120 by isothermal titration calorimetry. A and C Binding isotherms of AAR029b (A) and KR13 (C) to wild type (black), V255I (red) and V255I/S143N (green) monomeric gp120 variants. Heats were obtained at 25 °C by injection of 8 μL of PT (100 μM) into a sample cell of a VP-ITC containing 1.4 mL recombinant HxBc2 gp120 (6–8 μM). Solid lines represent fits to a single site binding model. B and D The thermodynamic parameters free energy (blue), enthalpy (red) and entropy (green) extracted from the fits to the AAR029b (B) and KR13 (D) titrations in A and C. The data shown in A and C are derived from a single binding experiment for each condition. The data shown in B and D and summarized in Table 3 are the mean and range of mean of two independent experiments

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