CONFORMATION OF A BIOLOGICALLY-ACTIVE C-TERMINAL HEXAPEPTIDE ANALOG OF THE PHEROMONE BIOSYNTHESIS ACTIVATING NEUROPEPTIDE BY NMR-SPECTROSCOPY

The solution conformation of a biologically active C-terminal hexapept ide analog of the pheromone biosynthesis activating neuropeptide Tyr-D -Phe-Ser-Pro-Arg-Leu-NH2 has been studied by NMR spectroscopy. A p-tur n conformation was identified from the NOE connectivities observed for the peptide in a mixed solvent of water and DMSO, indicating that thi s is the biologically active conformation of the peptide. This study a lso suggests that the use of such an aqueous-like solvent mixture allo ws the observation of a preferred conformation for small linear peptid es in the presence of conformational averaging. (C) Munksgaard 1994.