Structural requirements for the biological activity of enterostatin.

@article{Lin1994StructuralRF,
  title={Structural requirements for the biological activity of enterostatin.},
  author={Ling Lin and Setsuro Okada and David A. York and George A. Bray},
  journal={Peptides},
  year={1994},
  volume={15 5},
  pages={849-54}
}
A series of enterostatin analogues were tested to investigate the minimal structure required for activity to suppress the intake of high-fat (HF) diets. The dose-response curve to intracerebroventricular (ICV) enterostatin was U-shaped (maximal inhibition at 1 nmol). Removal or modification of the N-terminal valine from enterostatin (Val-Pro-Asp-Pro-Arg) abolished activity, as did C-terminal amidation. The tripeptide (Pro-Asp-Pro) and the cyclo-diketopiperazine cyclo-Asp-Pro retained activity… CONTINUE READING

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