Factors Impacting the Gastrointestinal Digestive Enzymes Fate of Magnesium Oxide Clusters: In Silico Characterization

Recently, metal oxide cluster dots have moved into medicinal and biological contemplations. Digestive system comprises different pH levels that may facilitate the formation of metal oxide clusters hypothetically. Those clusters may further interact with digestive system enzymes and generate metal cluster-enzyme protein complexes. The present study investigated the profiles of such 50 complexes using molecular docking techniques. A total of five magnesium oxide clusters-Mg₄O₄, Mg₅O₅, Mg₆O₆, Mg₇O₇, and Mg₈O₈-were designed, optimized, and docked with 10 human digestive system-related metalloenzymes (3P95, 4A94, 2V77, 2JBK, 1PJP, 1N1M, 1X0V, 1BSI, 1C8Q, 1ZLI). The complexes were produced using molecular docking simulations. The results revealed that the magnesium oxide cluster dots (MgO-CDs) show nonbonding interactions with different enzymes. The binding affinities of MgO clusters with enzymes ranged from -8.8 to -2.9 kcal/mol. The carboxypeptidase B (Protein Data Bank [PDB] ID: 1ZLI) and Mg₈O₈ exhibited most significant interactions with -8.8 kcal/mol and Ki 0.35 µM. Such interactions are helpful to understand the carboxypeptidase B (IZLI) enzymatic activity in hypermagnesemia symptoms, which leads to build up of non-degraded proteins.