We are currently working on development of iBodies directed towards whole protease families
A family of enzymes that cleaves peptide bonds in a single step proteolysis via utilization of an activated water molecule by one or more aspartate residues. Almost all aspartic proteases are inhibited by pepstatin. Pepsins, cathepsins and renins are representatives of the eukaryotic aspartic proteases.
Pepstatin based inhibitor
iBody KD = Ki (HIV-1 protease) = 19 n (measured with Surface Plasmon Resonance)
anti-aspartic protease family iBodies were used in methods such as bio-imaging with confocal microscopy, ELISA, protein immobilization and pull down from cell lysates (see the results below)
Tang, J. and Wong, R. N. S. (1987), Evolution in the structure and function of aspartic proteases. J. Cell. Biochem., 33: 53–63. doi:10.1002/jcb.240330106
Serine proteases (SerPR) are peptidases with a catalytic triad (His, Ser, Asp) in their active site. Two broad groups of these enzymes are the chymotrypsin-like and subtilisin-like proteases.
Pefabloc (4-(2-aminoethyl) benzenesulfonyl fluoride) based inhibitor
anti-serine protease family iBodies were used in methods such as bio-imaging with confocal microscopy, ELISA, protein immobilization, pull down from cell lysates and western blotting (see the results below)
Di Cera, E. (2009). Serine Proteases. IUBMB Life, 61(5), 510–515. http://doi.org/10.1002/iub.186