They say they are superior to existing mab's and also the new generation single chain antibodies. The foll is from an abstract from the recent nature magazine. I don't have full text though. It is one of the recent Aussie Bio's whose price didn't fall after the ipo...
Regards,
Praveen
Screening for peptide drugs from the natural repertoire of biodiverse protein folds
Paul M Watt
Phylogica Ltd., 105 Roberts Road, Subiaco, Perth, Western Australia 6008.
Correspondence should be addressed to Paul M Watt paulw@phylogica.com
Although monoclonal antibody (mAb) drugs targeting protein interactions exist, these therapeutics cannot access intracellular proteins involved in disease complexes. Moreover, mAbs are more difficult to deliver and are frequently associated with a prohibitive 'royalty stack.' Outlined here is an alternative approach based on libraries of natural, highly structured peptides that offers new opportunities for identifying effective, specific inhibitors of protein-protein interactions. Libraries of such peptides (referred to hereafter as phylomers) comprise both random and structured peptides encoded by natural genes of diverse bacterial genomes. Because the number of protein subdomain structures found in nature is limited, diverse libraries containing millions of phylomers constitute virtually all of the available classes of protein fold structures, providing a rich source of peptides that interact specifically and with high affinity to human proteins. This approach may help not only in understanding the implications of each interaction identified within the interactome but also in the development of effective drugs targeted to particular protein functions. Although phylomers are active in animal models, the challenge remains to demonstrate efficacy and safety in a clinical setting.
phylogica.com |
