Author(s)

Kou Takahashi¹, Ryotaro Miyazaki¹, Daisuke Nakane¹, Temitayo O. Aiyelabola², Takashiro Akitsu^1*

¹Department of Chemistry, Faculty of Science, Tokyo University of Science, Tokyo, Japan.
²Department of Chemistry, Faculty of Science, Obafemi Awolowo University, Ile-Ife, Nigeria.

Hydrophobic Val derivative Schiff base copper(II) complexes and dipeptide (AlaAla, GlyGly) derivative Schiff base copper(II) complexes were introduced into egg white lysozyme. X-ray crystal structure analysis revealed amino acid derivative Schiff base copper(II) complexes were obtained. Herein we discuss primarily on the binding mode of copper(II) of the complexes obtained with egg white lysozyme. The electron density of copper(II) ions was confirmed by X-ray crystal structure analysis. The Val derivative Schiff base copper(II) complex was weakly bound at Arg114 of egg white lysozyme. In other copper(II) complexes, binding of copper(II) ions with dissociated ligands to various residues was observed. The binding sites of copper(II) ions were compared with computational scientific predictions.

Copper, Schiff Base, Lysozyme, Metal-Protein Binding, Computational Methods

Takahashi, K. , Miyazaki, R. , Nakane, D. , Aiyelabola, T. and Akitsu, T. (2024) Preliminary Investigation of Copper(II) Ion Binding or Complex Coordination in Lysozeme Molecules. Journal of Materials Science and Chemical Engineering, 12, 98-103. doi: 10.4236/msce.2024.124008.