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.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Angewandte Chemie - International Edition |
| Vol/bind | 53 |
| Udgave nummer | 48 |
| Sider (fra-til) | 13020-13041 |
| Antal sider | 22 |
| ISSN | 1433-7851 |
| DOI | |
| Status | Udgivet - 2014 |
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