Molecular docking study of designed N-myristoyl transferase inhibitors

Abstract

N-myristoyl transferase has a key role in the myristoylation of vital proteins and is necessary for the growth and synthesis of material for the survival of various fungi. Due to the difference in the structure of fungal and mammalian N-myristoyl transferase, the crystal structure of the N-myristoyl transferase originating from Candida albicans was used as the target molecule. The present in silico study aims to design compounds, benzofuran derivatives, and simulate the interactions of the compounds and the amino acid sequences of the active center Nmyristoyl transferases from Candida albicans using the molecular docking method. The highest number of significant binding interactions is realized by the derivative 4. Affinity toward the Nmyristoyl transferase active site was very similar to the co-crystallized ligand, and important hydrogen interactions were retained. Based on the obtained results of molecular docking, it can be concluded that derivative 4 has the potential to inhibit N-myristoyl transferase, on which future research of its antifungal activity can be based.