Peptide fragments derived from the β-chain of hemoglobin (hemorphins) are centrally active in vivo

  title={Peptide fragments derived from the $\beta$-chain of hemoglobin (hemorphins) are centrally active in vivo},
  author={Thomas P. Davis and Terrence J. Gillespie and Frank Porreca},

Antinociceptive Effects of VV-Hemorphin-5 Peptide Analogues Containing Aminophosphonate Moiety in Mouse Formalin Model of Pain.

This study contributes to the elucidation of the role of Valine and the number of amino acid residues in the structure of hemorphin peptide analogs in their effectiveness in suppressing both acute and inflammatory experimental pain.

Radioligand binding properties of VV-hemorphin 7, an atypical opioid peptide.

The common -Arg-Phe sequence at the carboxyl terminal end, which is similar to those of other endogenous peptides in neuropeptide FF and FMRF-NH(2), brings attention to the C-terminal end of the molecule and points to the possible existence of a common nonopioid binding site in mammals.

The hemorphins: a new class of opioid peptides derived from the blood protein hemoglobin.

This article will review recent studies of the hemorphins regarding their structures, mechanisms for their release, and their biological actions and place a particular emphasis on their role in exercising human and their clinical relevance.

Opioid peptides derived from hemoglobin: hemorphins.

Investigation of hemoglobin peptic hydrolysate has revealed the presence of biologically active peptides with affinity for opioid receptors and the generation of VV-hemorphin-7 from globin by peritoneal macrophages.

Identification of functionally important dipeptide in sequences of atypical opioid peptides

In tests on ileum preparations of guinea pig and mouse vas deference in vitro, Tyr-Pro was devoid of opioid activity, which proved its indirect influence on opioid receptors.

Isolation of a heptapeptide Val-Val-Tyr-Pro-Trp-Thr-Gln (valorphin) with some opiate activity.

Bovine hypothalamic tissue was extracted and purified by solid phase extraction and several reversed-phase HPLC steps. The amino acid sequence of the purified peptide was determined by Edman



Bis-penicillamine enkephalins possess highly improved specificity toward delta opioid receptors.

  • H. MosbergR. Hurst T. Burks
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1983
The conformationally restricted, cyclic, disulfide-containing, enkephalin analogs and the bis-Pen-containing analogs provide an order of magnitude increase in delta receptor selectivity.

beta-Endorphin and its metabolites stimulate motility of the dog small intestine.

It is demonstrated that the small intestine can metabolize beta- endorphin into a number of active fragments which increase motility and suggest a regional specificity of enzymatic processing of beta-endorphin in the dog intestine.

Multiple endogenous opioid peptides

  • V. Höllt
  • Biology, Chemistry
    Trends in Neurosciences
  • 1983