Authors: Eunice Murage, Ph.D., and Miguel Castro, Ph.D., Affiliations: Bio-synthesis, Inc. 612 E. Main street, Lewisville, Tx 75057 USA
Peptides are attractive therapeutic agents for many diseases. However, poor cell permeability, short half life in vivo due rapid enzyme degradation has long been a major drawback in their clinical application. In order to overcome this, modification of peptides backbone has been of most interest. In particular, synthetic cyclic peptides are being investigated as potential drug candidates due to their improved cell permeability, enzyme stability, high receptor affinity and selectivity.
For instance, hydrocarbon stapled peptides has been shown to bind and inhibit the NOTCH1 transcription factor. NOTCH proteins have been shown to play a pivotal role in cellular differentiation, proliferation and apoptosis. Mutations in NOTCH1 have been linked with diseases like T-cell acute lymphoblastic leukemia.1
Thus constrained peptide assemblies would provide a good opportunity to explore the protein-protein interactions due their increased binding affinity compared to their linear counterparts. Due to the attractive biological properties offered by these modified peptides there is a growing demand in the current research in drug discovery,. In order to meet this demand Biosynthesis Inc. is now offering constrained peptides in form of stapled peptides and lactam bridge constrained peptides.
- Raymond E. M., Melanie C., Tina N. D., Cristina Del Bianco, Jon C. A., Stephen C. B., Andrew L. K., D. Gary G., Gregory L. V., James E. B., Nature 2009, 462, 182-188.
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