CMD Bioscience Achieves Proof Of Concept For It's Proprietary Peptide Computational Discovery Platform

CMDBioscience, a CT based biotechnology company specializing in computer-aided peptide drug discovery, announced today the completion of a research collaboration aimed at identifying novel peptide antagonists of the dengue virus using the CMDBioscience proprietary computational peptide drug discovery platform. End Quote

New Haven-Meriden, CT (1888PressRelease) November 16, 2010 - Using the CMDBioscience proprietary computational peptide discovery platform, CMD scientists were able to model and optimize a structure of the dengue viral target and evaluate over 480,000 novel peptide ligand sequences, ultimately converging on the 27 most promising sequences. The computational phase of the project was completed in seven weeks. Subsequent synthesis and experimental testing of the 27 novel peptide designs revealed excellent anti-infective activity for 5 of the designed peptide ligands.

"We are very excited about the results from this research collaboration, as it definitively demonstrates that by using our computational discovery platform we can discover truly novel peptides for our partner organizations in a very short period of time. We have been confident all along that this technology is groundbreaking and this collaboration provides that validation," stated Dr. Joseph Audie, co-founder and CEO of CMDBioscience. "There is a pressing need for computational discovery tools focused on peptide therapeutics, and CMDBioscience offers a unique, rigorous, and compelling solution for our biotech and pharmaceutical partners."

About: CMDBioscience is a computational biotechnology company that specializes in the computer-enabled analysis, modeling and design of therapeutic protein-peptide interactions or structure-based peptide design. Using structure-based peptide design, CMD scientists can help partner organizations efficiently identify novel peptide hits and leads, understand the structural basis of protein-peptide interactions, and rationally optimize peptide leads.

http://www.cmdbioscience.com

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