DFT Calculations, ADME Analysis and Molecular Docking Studies of the Compound AHTPO With the Digestive Enzyme Trypsin Found in Cold-Adapted Fish Species

For the special amine 7-Amino-3-(4-aminophenyl)-5H-thiazolo[3,2-a]pyrimidin-5-one (AHTPO), previously reported experimental biological activities served as the foundation for further studies. Computational chemistry and molecular simulation techniques were subsequently applied to investigate AHTPO. Its interactions with trypsin enzymes derived from cold-adapted fish species were examined. The compound's biological activity and pharmacokinetic properties were assessed using DFT calculations, molecular docking, and ADME analyses. Molecular docking results indicated that AHTPO exhibits strong binding affinities with the 1A0J and 2TBS enzymes, with the binding to 2TBS being energetically more favorable. Additionally, ADME analysis revealed that while the AHTPO shows potential for pharmaceutical applications, its gastrointestinal absorption and blood-brain barrier permeability may present certain limitations. Regarding its electronic and optical properties, AHTPO's high dipole moment and polarizability values enhance its flexibility and adaptability in biological environments. The HOMO-LUMO energy gap suggests that the AHTPO achieves a balance between stability and reactivity, enabling high activity in biomolecular interactions. These findings highlight the promising pharmacological potential of AHTPO in binding with trypsin enzymes, suggesting its viability as a therapeutic agent.