Cyclic Analogues of Proline-Rich Protein Fragments : Part II : Conformational Studies Using NMR Spectroscopy and Theoretical Conformational Analysis

These peptides were designed based on the immunoregulatory activity of linear peptides obtained after chymotrypsin digestion of PRP. Despite the fact that the structures of both analogues cannot be interpreted in terms of a single conformation, the superposition of the most populated conformations of the cyclic peptides studied revealed a similar geometry for the Tyr-Val-pro-Leu-Phe-Pro fragment (RMSD=1.6 A) in both peptides and therefore might be considered to be responsible for the biological activity.