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The present study gives an overview of the binding energetics of the homologous heterodimers of cruzipain-chagasin based on the binding energy (Δ G  b ) prediction obtained with FoldX. This analysis involves a total of 70 homologous models of the cruzipain-chagasin complex which were constructed by homology from the combinatory variation of nine papain-like cysteine peptidase structures and seven cysteine protease inhibitor structures (as chagasin-like and cystatin-like inhibitors). Only 32 systems have been evaluated experimentally, Δ G  b  experimental values previously reported. Therefore, the result of the multiple analysis in terms of the thermodynamic parameters, are shown as relative energy |ΔΔ G | = |Δ G  b  from  FoldX - Δ G  b  experimental |. Nine models were identified that recorded |ΔΔG| &lt; 1.3, five models to 2.8 &gt; |ΔΔG| &gt; 1.3 and the other 18 models, values of |ΔΔ G | &gt; 2.8. The energetic analysis of the contribution of Δ H and Δ S to Δ G  b to the 14-molecular model presents a Δ G  b mostly Δ H -driven at neutral pH and at an ionic strength ( I ) of 0.15 M. The dependence of Δ G  b ( I ,pH) at 298 K to the cruzipain-chagasin complex predicts a linear dependence of Δ G  b ( I ). The computational protocol allowed the identification and prediction of thermodynamics binding energy parameters for cruzipain-chagasin-like heterodimers.

In Silico Analysis of Homologous Heterodimers of Cruzipain-Chagasin from Structural Models Built by Homology