Solid-phase syntheses of beta-turn analogues to mimic or disrupt protein-protein interactions

Authors
Citation
K. Burgess, Solid-phase syntheses of beta-turn analogues to mimic or disrupt protein-protein interactions, ACC CHEM RE, 34(10), 2001, pp. 826-835
Citations number
67
Categorie Soggetti
Chemistry & Analysis",Chemistry
Journal title
ACCOUNTS OF CHEMICAL RESEARCH
ISSN journal
00014842 → ACNP
Volume
34
Issue
10
Year of publication
2001
Pages
826 - 835
Database
ISI
SICI code
0001-4842(200110)34:10<826:SSOBAT>2.0.ZU;2-8
Abstract
Protein-protein interactions are difficult targets in medicinal chemistry, but they will become increasingly important as data from The Human Genome P roject is interpreted. Our work focuses on beta -turn mimics that are desig ned to mimic or disrupt some of these interactions. Solid-phase syntheses a nd preferred conformations of beta -turn mimics that incorporate dipeptide units are discussed. The activity of one illustrative compound that potenti ates the interaction of the nerve growth factor with its transmembrane tyro sine kinase receptor TrkA is outlined. Finally, the importance of dimeric t urn mimics and some new approaches to these are described.