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Valorphin

Valorphin, also known as VV-hemorphin-5, is a naturally occurring, endogenous opioid heptapeptide of the hemorphin family with the amino acid sequence H-Val-Val-Tyr-Pro-Trp-Thr-Gln-OH (VVYPWTQ). It is produced in the body via proteolyic cleavage of residues 33-39 of the β-chain of hemoglobin. Valorphin binds preferentially to the μ-opioid receptor and produces effects such as analgesia and self-administration in animals. It also possesses cytotoxic and antiproliferative properties against tumor cells, the mediation of which, because they are reversed by naloxone, appears to be dependent on the opioid receptors.

References

References

  1. (February 1985). "Valorphin: a novel chemical structure with opioid activity". Neuropeptides.
  2. (June 1992). "Isolation of a heptapeptide Val-Val-Tyr-Pro-Trp-Thr-Gln (valorphin) with some opiate activity". International Journal of Peptide and Protein Research.
  3. (May 2002). "Family of hemorphins: co-relations between amino acid sequences and effects in cell cultures". Peptides.
  4. (August 2002). "Antiproliferative action of valorphin in cell cultures". Journal of Peptide Science.
  5. (1997). "Tumor cell cytolysis mediated by valorphin, an opioid-like fragment of hemoglobin beta-chain". Peptides.
  6. (January 2005). "Antitumor effect of valorphin in vitro and in vivo: combined action with cytostatic drugs". Cancer Biology & Therapy.
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