title: Conformational studies of peptide cyclo-(D-Val-L-Pro-L-Val-D-Pro]3, a cation-binding analogue of valinomycin.
abstract: The solution conformation of cyclo-[D-Val-L-Pro-L-Val-D-Pro]3 (PV) and its alkali-metal ion complexes was investigated by proton nuclear magnetic resonance spectroscopy. It is concluded that the cation complexes of PV have S6 symmetry and are essentially isostructural with the K complex of valinomycin. In contrast to valinomycin, the Li- and Na-PV complexes are stable in methanol and have dissociation rate constants that are several orders of magnitude slower than the corresponding valinomycin complexes. Also in contrast to valinomycin, free PV exists in two different conformational states which interconvert at very slow rates (less than 1 s-1). One of these conformers has S6 symmetry and is structurally similar to that of the cation complexes. The other species, which has lower symmetry than S6, is the more stable conformer. Depending upon concentration and solvent polarity, the latter represents between 50 and 75% of the total mixture. It is proposed that PV may have a higher affinity for cations than valinomycin because of its higher potential energy in the uncomplexed state.
mesh_terms: D002414:Cations, Monovalent; D002586:Cesium; D004355:Drug Stability; D008094:Lithium; D009682:Magnetic Resonance Spectroscopy; D010456:Peptides, Cyclic; D011188:Potassium; D011392:Proline; D011485:Protein Binding; D011487:Protein Conformation; D011522:Protons; D012413:Rubidium; D012964:Sodium; D013691:Tellurium; D014633:Valine; D014634:Valinomycin / Q000031:analogs & derivatives*
chemical_list: D002414:Cations, Monovalent; D010456:Peptides, Cyclic; D011522:Protons; D002586:Cesium; D014634:Valinomycin; D011392:Proline; D008094:Lithium; D012964:Sodium; D014633:Valine; D012413:Rubidium; D013691:Tellurium; D011188:Potassium