Evaluation of in silico ADMET analysis and human serum albumin interactions of a new lanthanum(III) complex by spectroscopic and molecular modeling studies

A new lanthanum(III) complex, [La(Phe)(3)(H2O)(2)] (Phe = phenylalanine), was synthesized. The complex was characterized by elemental analysis, conductivity measurement, Fr-IR, UV/Vis and H-1 NMR techniques. Drug-like properties of this complex was evaluated through in silico ADMET predictions. The reactivity of this complex to human serum albumin (HSA) under simulated physiological conditions was studied by spectroscopic and molecular docking analysis. The fluorescence quenching of protein by addition of La(III) complex was due to static quenching mechanism. The thermodynamic parameters show that the binding process was spontaneous and that hydrogen bonds and hydrophobic forces play a major role in the association of the HSA-La(III) complex. Binding parameters between La(III) complex and protein such as binding sites number (n similar to 1) and binding constant (K-a similar to 10(4) M-1) were determined. The conformational changes of protein secondary structure in the presence of above complex were demonstrated by FT-IR, three-dimensional fluorescence and UV-Vis absorption techniques. Molecular docking of La(III) complex relating to HSA was investigated and confirmed the experimental results. All these experimental and computational results clarified that La(III) complex could bind with HSA effectively, which could be a useful guideline for efficient drug design. (C) 2017 Elsevier B.V. All rights reserved.