Conformational behavior of the linear hexapeptide senktide: A receptor specific tachykinin analog
Sumner, S., & Ferretti, J. A. (1989). Conformational behavior of the linear hexapeptide senktide: A receptor specific tachykinin analog. FEBS Letters, 253(1-2), 117-120. DOI: 10.1016/0014-5793(89)80942-1
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 ?-pleated sheet. The observed senktide-receptor specificity is suggested to result from a selection of this or a closely related conformation.