Interaction of DNA with small molecules: Role of copper histidyl peptide complexes in DNA binding and hydrolytic cleavage

Abstract

Deoxyribonucleic acid is the site of storage and retrieval of genetic information through interaction with proteins and other small molecules. Hydrolysis of the phosphodiester bond of DNA is of critical importance at several stages in a cell cycle. Thus, the development of metal complexes that cleave nucleic acids hydrolytically at physiological conditions is of great interest in the field of artificial metallonucleases. Among transition metals, Cu(II) complexes have been extensively studied in promoting hydrolysis of DNA. Histidine is a biologically important ligand for Cu(II) binding in many biological systems. Since imidazole is an efficient catalyst for ester hydrolysis at neutral pH and histidine residues are often involved in neutral hydrolytic metalloenzyme active centres and have the potential to bind to DNA, an attempt is made in this review to highlight the importance of DNA binding and cleavage and the role of a few copper histidyl peptide complexes in DNA binding and hydrolytic cleavage.