Figure 7
From: Potent anticancer activity of cystine-based dipeptides and their interaction with serum albumins
Energy spectrum distribution of the bound conformations for HSA (A) and BSA (C). All the best output from 100 independent docking simulations were arranged according to their binding energy. Very low energy conformations indicate thermodynamically favorable interaction. Binding of 1C and 1D with both the HSA and BSA were found to be better than that of 1A and 1B. But the inconsistency in the low energy binding modes suggests nonspecificity. Clustering of the bound conformations for HSA (B) and BSA (D). Binding modes within 2 Å standard deviation and 0.5 kcal mol-1 energy tolerance levels were clustered together. Although the low energy binding modes are prevalent no significant clustering was observed again suggesting no specificity in binding.