期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 21, 期 14, 页码 4051-4057出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2012.11.023
关键词
Protein-protein interactions; Secondary structure mimics; Computational design; Hot spot residues; Rational design
资金
- 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
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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