V- type proton ATP-ase to target cancer cells with the aid of Cyanobacterial metallothionein

Abstract

ATP-ases are a group of enzymes that utilizes ATP hydrolysis, and the subsequent release of energy, to achieve a cellular function. The cellular functions involving ATP-ases are plentiful and diverse including initiation of DNA replication, DNA repair and remodeling, protein folding and chaperoning, protein degradation, intracellular transport, and ion transport. A large number of these enzymes represent attractive drug targets, and drugs targeting ATP-ases, such as proton pump inhibitors. Two families of molecular chaperones, heat shock protein 90 and heat shock protein 70, possess N-terminal nucleotide binding domains (NBD) and require ATP-ase activity for their functions. NBD is charged and highly polar in nature and there is no crystal structure yet published. These two families of ATP-ases represent significant therapeutic targets for the treatment of cancer. The ATP-ase activity of Hsp90, in interaction to Cyanobacterial mettalothionein is essential for targeting cancer affected cells and can be used highly as a drug targeting molecule. Inhibition of ATP-ase activity at nucleotide binding site of the Hsp90 leads to prevent tumor growth. Till now, only two antibiotics (ansamycin and geldanamycin) were discovered for inhibiting ATP-ase enzymes. This article discuss about Vtype proton ATP-ases, interaction with Cyanobacterial mettalothionein for targeting cancer spoiled cells in Cancer treatment.