Abstract
Many proteins exert their biological activities through small exposed surface regions called epitopes that are folded peptides of well-defined three-dimensional structures. Short synthetic peptide sequences corresponding to these bioactive protein surfaces do not form thermodynamically stable protein-like structures in water. However, short peptides can be induced to fold into protein-like bioactive conformations (strands, helices, turns) by cyclization, in conjunction with the use of other molecular constraints, that helps to fine-tune three-dimensional structure. Such constrained cyclic peptides can have protein-like biological activities and potencies, enabling their uses as biological probes and leads to therapeutics, diagnostics and vaccines. This Review highlights examples of cyclic peptides that mimic three-dimensional structures of strand, turn or helical segments of peptides and proteins, and identifies some additional restraints incorporated into natural product cyclic peptides and synthetic macrocyclic pepti-domimetics that refine peptide structure and confer biological properties.
| Original language | English |
|---|---|
| Journal | Angewandte Chemie - International Edition |
| Volume | 53 |
| Issue number | 48 |
| Pages (from-to) | 13020-13041 |
| Number of pages | 22 |
| ISSN | 1433-7851 |
| DOIs | |
| Publication status | Published - 2014 |
Keywords
- Cyclic peptides
- Helices
- Macrocycles
- Natural products
- Peptidomimetics
