NMR and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles.
To better understand the structural basis of the biological activity of the neuropeptide substance P SP; (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2), two-dimensional nmr spectroscopy experiments and simulated annealing calculations were used to investigate the conformation adopted in the presence of the membrane model system sodium dodecyl sulfate. It was determined that SP in the presence of SDS micelles undergoes a conformational equilibrium between an alpha- and a 3(10)-helix involving the midregion (Pro4-Gln5-Gln6-Phe7-Phe8) of the peptide. The C-terminus adopts an extended conformation while the N-terminus remains quite flexible. The conformation adopted by SP in the presence of SDS micelles yields a structure that is consistent with the model of a neurokinin-1 selective ligand proposed by Convert.
Young
J K
JK
Department of Chemistry, Mississippi State University, Mississippi 39762.
Anklin
C
C
Hicks
R P
RP
D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012967:Sodium Dodecyl Sulfate; D013373:Substance P / Q000737:chemistry*
D008823:Micelles; D013373:Substance P; D012967:Sodium Dodecyl Sulfate