1252796-73-8Relevant articles and documents
Fluorescent analogues of the insect neuropeptide helicokinin I: Synthesis, photophysical characterization and biological activity
Chen, Heru,Scherkenbeck, Juergen,Zdobinsky, Tino,Antonicek, Horst
, p. 431 - 436 (2010)
In insects numerous physiological processes are regulated by neuropeptides. Two fluorescent analogues of the amino acids tryptophan and tyrosine were synthesized and incorporated in the diuretic neuropeptide helicokinin I from the moth Heliothis zea. By fluorescence emission measurements it was shown that both fluorescent helicokinin I analogues react sensitive on the dielectricity of their microenvironment. A helicokinin I analogue containing the fluorescent tryptophan mimic β-[6'-(N,N-dimethyl)-amino-2'-naphthoyl]alanine (Ald) was shown to bind to dodecylphosphocholine (DPC) micelles by the Ald residue. A membrane binding model for helicokinin I is proposed based on data from related mammalian and insect-neuropeptides.