1. Crystal Structure, Theoretical Analysis, and Protein/DNA Binding Activity of Iron(III) Complex Containing Differently Protonated Pyridoxal- S -Methyl-Isothiosemicarbazone Ligands.
- Author
-
Jevtovic V, Golubović L, Alshammari B, Alshammari MR, Rajeh SY, Alreshidi MA, Alshammari OAO, Rakić A, and Dimić D
- Subjects
- Ligands, Humans, Crystallography, X-Ray, Thiosemicarbazones chemistry, Thiosemicarbazones metabolism, Cattle, Coordination Complexes chemistry, Coordination Complexes metabolism, Animals, Protons, Ferric Compounds chemistry, Serum Albumin, Human chemistry, Serum Albumin, Human metabolism, Binding Sites, Iron chemistry, Iron metabolism, Protein Binding, Molecular Docking Simulation, DNA chemistry, DNA metabolism, Serum Albumin, Bovine chemistry, Serum Albumin, Bovine metabolism
- Abstract
Pyridoxal- S -methyl-isothiosemicarbazone (PLITSC) is a member of an important group of ligands characterized by different complexation modes to various transition metals. In this contribution, a new complex containing two differently protonated PLITSC ligands ([Fe(PLITSC-H)(PLITSC)]SO
4 )∙2.5H2 O was obtained. The crystal structure was solved by the X-ray analysis and used further for the optimization at B3LYP/6-311++G(d,p)(H,C,N,O,S)/def2-TZVP(Fe) level of theory. Changes in the interaction strength and bond distance due to protonation were observed upon examination by the Quantum Theory of Atoms in Molecules. The protein binding affinity of [Fe(PLITSC-H)(PLITSC)]SO4 towards transport proteins (Bovine Serum Albumin (BSA) and Human Serum Albumin (HSA)) was investigated by the spectrofluorimetric titration and molecular docking. The interactions with the active pocket containing fluorescent amino acids were examined in detail, which explained the fluorescence quenching. The interactions between complex and DNA were followed by the ethidium-bromide displacement titration and molecular docking. The binding along the minor groove was the dominant process involving complex in the proximity of DNA.- Published
- 2024
- Full Text
- View/download PDF