Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 13, Issue 1, Pages 11-16Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2004.09.009
Keywords
foldamer; helix; proteomics; protein recognition
Funding
- NIGMS NIH HHS [R01 GM074756-04, R01 GM074756] Funding Source: Medline
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We became interested several years ago in exploring whether 14-helical beta-peptide foldamers could bind protein surfaces and inhibit protein-protein interactions, and if so, whether their affinities and specificities would compare favorably with those of natural or miniature proteins. This exploration was complicated initially by the absence of a suitable beta-peptide scaffold, one that possessed a well-defined 14-helical structure in water and tolerated the diverse sequence variation required to generate high-affinity protein surface ligands. In this perspective, we describe our approach to the design of adaptable beta-peptide scaffolds with high levels of 14-helix structure in water, track the subsequent development of 14-helical beta-peptide protein-protein interaction inhibitors, and examine the potential of this strategy for targeting other therapeutically important proteins. (C) 2004 Elsevier Ltd. All rights reserved.
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