Conformational behavior of the linear hexapeptide senktide: a receptor specific tachykinin analog.
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.
Sumner
S C
SC
Laboratory of Chemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.
Ferretti
J A
JA
D000577:Amides; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments; D011487:Protein Conformation; D013373:Substance P / Q000031:analogs & derivatives*
D000577:Amides; D010446:Peptide Fragments; C054724:senktide; D013373:Substance P