Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 21, Issue 14, Pages 4051-4057Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2012.11.023
Keywords
Protein-protein interactions; Secondary structure mimics; Computational design; Hot spot residues; Rational design
Funding
- National Institutes of Health [GM073943]
- National Science Foundation [CHE-1151554]
- New York University
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1151554] Funding Source: National Science Foundation
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Development of specific ligands for protein targets that help decode the complexities of protein-protein interaction networks is a key goal for the field of chemical biology. Despite the emergence of powerful in silico and experimental high-throughput screening strategies, the discovery of synthetic ligands that selectively modulate protein-protein interactions remains a challenge for bioorganic and medicinal chemists. This Perspective discusses emerging principles for the rational design of PPI inhibitors. Fundamentally, the approach seeks to adapt nature's protein recognition principles for the design of suitable secondary structure mimetics. (C) 2012 Elsevier Ltd. All rights reserved.
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