Abstract
Macrocyclic constraints are often employed to rigidify the conformation of flexible oligomeric systems. This approach has recently been used to organize the structure of peptoid oligomers, which are peptidomimetics composed of chemically diverse N-substituted glycine monomer units. In this review, we describe advances in the synthesis and characterization of cyclic peptoids. We evaluate how the installation of covalent constraints between the oligomer termini or side chains has been effective in defining peptoid conformations. We also discuss the potential applications for this promising family of macrocyclic peptidomimetics.
Original language | English (US) |
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Pages (from-to) | 5528-5537 |
Number of pages | 10 |
Journal | Chemistry - A European Journal |
Volume | 16 |
Issue number | 19 |
DOIs | |
State | Published - May 17 2010 |
Keywords
- Foldamers
- Macrocycles
- Peptidomimetics
- Peptoids
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Organic Chemistry