Jh. Gao et al., CONFORMATIONAL STUDIES OF ASTERIN-B AND A STERIN-C IN SOLUTION BY NMR.2. CONFORMATIONAL-ANALYSIS BY NMR AND MOLECULAR DYNAMIC SIMULATIONS, Huaxue xuebao, 54(7), 1996, pp. 702-708
The conformational properties of two pentapeptides Asterin B(Delta Pro
- Thr - Ser - beta Phe - Abu - OMe, 1) and Asterin C(Delta Pro - Abu
- Ser - beta Phe - Thr - OMe, 2), isolated from Chinese traditional me
dicine Aster tataricus, have been investigated by 2D - NMR and restrai
ned molecular dynamic calculations (RMD). The solution conformation of
1 was characterized as a nonclassic beta- turn structure at(Delta Pro
- Thr - Ser - beta Phe) region with an amphiphilic feature, which may
be related to its antitumor activity against P388 leukemia. There is
no evidence in the form of lowered amide proton temperature coefficien
ts for direct hydrogen bonding as a primary source of turn stability.
Instead, the major stabilization appears to be the hydrophobic interac
tion between aromatic rings (Delta Pro and beta Phe). Implications for
stabilization of this unusual turn structure during the earliest even
ts in protein folding are discussed. The conformation of 2 in solution
was shown to be more flexible with multiple conformational averaging.