title: Conformational behavior of the linear hexapeptide senktide: a receptor specific tachykinin analog.
abstract: A receptor selective linear hexapeptide tachykinin analog, senktide, is shown to be highly ordered in solution. The conformational restriction is attributed to steric and electrostatic interactions produced by N-methylation of the third amino acid residue in the sequence and the negatively charged N-terminus. The structure of senktide is described as a dynamic mixture of similar conformations where the predominant one is a distorted antiparallel hydrogen bonded beta-pleated sheet. The observed senktide-receptor specificity is suggested to result from a selection of this or a closely related conformation.
authors: Laboratory of Chemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.
authors: S C
authors: SC
authors: Sumner
authors: J A
authors: JA
authors: Ferretti
mesh_terms: D000577:Amides; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments; D011487:Protein Conformation; D013373:Substance P / Q000031:analogs & derivatives*
chemical_list: D000577:Amides; D010446:Peptide Fragments; C054724:senktide; D013373:Substance P