Topological study of interactions between some inhibitors and ALK-5 using QTAIM methodology

Activin kinase type 5 (ALK-5) is a biological target related to some types of cancer, such as breast cancer, being that the inhibition of this target is a strategy that has been studied as a way to treat cancer. Therefore, the objective of this work is to use the computational chemistry to evaluate the main interactions that occur between the main residues at the active site of ALK-5 (Lys232, Glu245, Tyr249, His283, Asp351 and one structural water) and six inhibitors of this biological target1,2. In this way, the intermolecular hydrogen bonds that occur between the six inhibitors and the active site of ALK-5 were evaluated using the QTAIM method (AIMALL software)3,4. Table 1 shows the values of electron density (ρ) and Laplacian of electron density (∇2ρ) for bonds critical points (BCPs) for these interactions.