Study of L-tryptophan (a neurotransmitter precursor): spectral, Hirshfeld surface, molecular docking and dynamics simulations

Abstract

Abstract This paper describes both theoretical and empirical studies on essential amino acids and the serotonin precursor L-tryptophan. To analyze the molecular structure, the FTIR technique 1H NMR, and ultraviolet–visible spectroscopy were performed. The current research used the DFT – B.3.L.Y.P/6-311++G(d,p) methodology to enhance an essential amino acid in the electronic ground state. The spectral studies of the chosen compound were analyzed in gaseous state and various solvent phases, and the outputs were then related with observed experimental information using the Time dependent-DFT methodology. NBO analysis was employed to determine the stabilization energies and electronic transitions. MEP and ELF analyses were accomplished to understand the chemically responsive regions of molecule. Thermodynamic functions of the title chemical are also known at various temperatures. 3D Hirshfeld surface studies and two-dimensional fingerprint images were utilized to offer a thorough explanation of the crystal surface’s interactions with other molecules. To investigate protein-ligand interactions, least binding energy was measured as −7.2 kcal mol−1 in molecular docking. L-Trp and its derivatives were also investigated for drug-likeness, and all substances were found to be of a comparable behavior. Precisely an outcome, this compound could be useful in the advancement of therapies.