Polyoxometalates as a novel class of artificial enzymes: insight into the molecular interactions with proteins and peptides.

Selective cleavage of peptides and proteins is one of the most required and most important procedures in biochemical and bioengineering practice. Several proteolytic enzymes are available for this purpose. Unfortunately, they are characterized by some seious short-comings. They are usually not regioselective and produce short fragments which are difficult to identify. Chemicals that mediate protein cleavage offer an attractive alternative to proteolytic enzymes. However, they often require harsh conditions and tend to cleave proteins with partial selectivity and low yields. Clearly, there is a need for the development of new and efficient agents that could greatly facilitate the study of protein structure and function. The conceptually new way for creating a regioselective, tuneable, and non-invasive synthetic protease has been recently achieved in our lab by using polyoxometalate (POM) skeletons as ligands for hydrolytically active metal ions. Our studies have shown that at physiological pH Wells-Dawson and Keggin type POMs hydrolyzed human serum albumin and lysozyme in a selective manner. The aim of this study is to obtain insight into this novel reaction on a molecular level by using a range of different techniques. The information obtained from these studies will be essential to establish the structure-activity relationship and tune the selectivity of these novel cleavage agents.

Keywords:Artificial peptidase, Polyoxometalates, Proteins, Hydrolytically active metal ions

Disciplines:Other engineering and technology