期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 54, 期 31, 页码 8896-8927出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201412070
关键词
inhibitors; peptides; peptidomimetics; protein-protein interactions
资金
- AstraZeneca
- Bayer CropScience
- Bayer HealthCare
- Boehringer Ingelheim
- Merck KGaA
- Max Planck Society
- BMBF (Bundesministerium fur Bildung und Forschung
- Medizinische Chemie in Dortmund) [BMBF 1316053]
- Deutsche Forschungsgemeinschaft (DFG
- Emmy Noether program) [GR3592/2-1]
Protein-protein interactions (PPIs) are involved at all levels of cellular organization, thus making the development of PPI inhibitors extremely valuable. The identification of selective inhibitors is challenging because of the shallow and extended nature of PPI interfaces. Inhibitors can be obtained by mimicking peptide binding epitopes in their bioactive conformation. For this purpose, several strategies have been evolved to enable a projection of side chain functionalities in analogy to peptide secondary structures, thereby yielding molecules that are generally referred to as peptidomimetics. Herein, we introduce a new classification of peptidomimetics (classes A-D) that enables a clear assignment of available approaches. Based on this classification, the Review summarizes strategies that have been applied for the structure-based design of PPI inhibitors through stabilizing or mimicking turns, -sheets, and helices.
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