Cleavage of proteins by a mixed-ligand copper(II) phenolate complex: hydrophobicity of the diimine co-ligand promotes cleavage.
The mixed-ligand copper(II) complex [Cu(tdp)(tmp)](ClO4), where H(tdp) is 2-[(2-(2-hydroxyethylamino)ethylimino)methyl]phenol and tmp is 3,4,7,8-tetramethyl-1,10-phenanthroline, exhibits cleavage of the proteins bovine serum albumin and lysozyme, producing approximately 5 and 4 kDa protein fragments respectively within a few minutes at micromolar concentrations. The hydrophobic tmp ligand recognizes the hydrophobic site and enhances protein binding and cleavage even at physiological pH and temperature.
Rajendiran
Venugopal
V
School of Chemistry and National Facility for Marine Cyanobacteria, Bharathidasan University, Tiruchirappalli 620024, India.
Palaniandavar
Mallayan
M
Swaminathan
Palanisami
P
Uma
Lakshmanan
L
D000818:Animals; D002417:Cattle; D003300:Copper / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D007097:Imines / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D010636:Phenols / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*
D007097:Imines; D008024:Ligands; D010636:Phenols; D011506:Proteins; D003300:Copper