Constrained peptides - a new therapeutic approach for drug design

Synthetic locked polypeptides, breakthrough peptide mimicry for intracellular protein-protein interactions, have been shown to increase biological activity, potency in cancer cell death in vivo and can be therapeutically beneficial for preclinical mo
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Lewisville, TX ( February 8, 2011 - Lewisville, TX, January 2011 - Fundamental biological processes such as cell growth, cell cycle, metabolic pathways and signal transduction are essential in living organisms to maintain life. These processes are normally regulated by proteins through a process called protein-protein interactions (PPI).

For decades, researchers have sought to understand intracellular PPI interactions since these interactions mediate numerous disease states like cancer, neurological disorder and biological mechanisms underlying the pathogenesis of bacterial and viral infections. Researchers have recently focused on designing modified peptides and small molecules which have superior properties than the native peptides. Particularly, synthetic modified peptides offer a better approach since they resemble native hormones and thus cannot trigger immune response once administered to the body. In addition, the availability of cheap and readily available amino acid residues, automated processes and diversified chemistry for synthesizing peptides, have resulted to increased demand for modified peptides in various clinical applications.

Constrained peptides are peptides with cyclic portions that contain the biologically active site that is vital to intracellular protein to protein interactions. The theory behind it is that, once the peptide has been locked into a specific conformation by either lactam bridge or `stapling', the conformation freedom is decreased resulting to increased binding affinity and biological activity to the targeted areas. When these constraints are strategically placed on a peptide, the constrained peptide may have a higher biological activity and efficient cell permeability which is not the case with unconstrained peptides. In addition, these peptides have longer circulation life time in the body because their unique structure blocks proteolysis which is one of the major shortcomings in therapeutic application of native peptides.

Miguel Castro, Ph.D., CEO of Bio-Synthesis describes how his company can provide this technology, "Recently, Bio-Synthesis launched 'positional cyclization' scanning techniques to our systematic peptide library screening service tools. This new tool will provide a conceptual approach towards designing of peptidomimetics and small molecules for drug discovery. We have the experience, the skills and the technology to deliver high quality products to our clients".

Bio-Synthesis Incorporated has been serving the life science community since 1984. Bio-Syn specializes in constructing such bio-conjugates as peptides, DNA, RNA and small-molecule drugs. Bio-Synthesis has one of the largest peptide synthesis facilities in the U.S. and can provide different types of synthetic DNA, peptides of over 150 residues, antibodies, bio-conjugates, analyte-specific reagents and many other products and services. Bio-Synthesis, Inc. is a leading CRO headquartered in Lewisville, Texas.

Integrated solutions spanning across genomics, proteomics and cell biology.

© 2010 Bio-Synthesis, Inc. All rights reserved.


Tag Words: custom peptides, peptides
Categories: Scientific

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