An In Silico Study of the Interactions of Alkaloids from Cryptolepis sanguinolenta with Plasmodium falciparum Dihydrofolate Reductase and Dihydroorotate Dehydrogenase

Figure 11

Binding conformation predicted from molecular docking was stable under dynamic conditions. (a) Trajectory showing stability of protein ligand complexes for qm-PfDHFR. High steric advantage of cryptomisrine (brown line) enhanced interactions with pocket residues, hence an overall reorganization of the starting structure to attain an effective binding conformation (RMSD between 13 ns and 50 ns of the trajectory fluctuated in the range between 0.5 nm and 1.3 nm). (b–e) Interacting residues contributing to binding affinity have been colored based on b-factors. Neocryptolepine-Asp54 interaction contributed to overall complex stability.

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