Optimization of Proteolytic Cleavage of Peptide Affinity

We will develop a peptide cleavage system which will improve the efficiency and specificity of cleatag peptides from recombinant proteins. The purpose is to simplify the purification of recombinant pprokaryotic or eukaryotic expression systems and ensure no additional terminal amino acids will remaproduct. Although fusion tag peptides and peptidases are commercially available, the efficiency andis not optimal and often results in low yields of the desired protein product. Development of an optwill impact research labs as well as therapeutics and production processes by increasing the efficieproteins and reducing the cost of protein production. A selectable M13 filamentous phage display sysidentify optimal combinations of cleavage sites and peptidases. Two approaches will be pursued: onecleavage site, and the other targeting the enzymatic domain of the peptidase.