Structure-activity studies on prolactin-releasing peptide (PrRP). Analogues of PrRP-(19-31)-peptide

J Pept Sci. 2005 Mar;11(3):161-5. doi: 10.1002/psc.612.


An investigation of a series of single replacement analogues of PrRP-(19-31)-peptide has shown that good functional activity was retained when Phe31 was replaced with His(Bzl), Phe(4Cl), Nle, Trp, Cys(Bzl) or Glu(OBzl); when Val28 or Ile25 was replaced with Phg; when Gly24 was replaced with D-Ala, L-Ala, Pro or Sar; when Ser22 was replaced with Gly and when Ala21 was replaced with Thr or MeAla. The results confirm that the functionally important residues are located within the carboxyl terminal segment, -Ile-Arg-Pro-Val-Gly-Arg-Phe-NH2.

MeSH terms

  • Amino Acid Sequence
  • Calcium Signaling / drug effects
  • Cell Line
  • Cyclization
  • Disulfides / chemistry
  • Humans
  • Hypothalamic Hormones / chemistry*
  • Hypothalamic Hormones / pharmacology*
  • Inhibitory Concentration 50
  • Molecular Sequence Data
  • Neuropeptides / chemistry*
  • Neuropeptides / pharmacology*
  • Prolactin-Releasing Hormone
  • Structure-Activity Relationship


  • Disulfides
  • Hypothalamic Hormones
  • Neuropeptides
  • PRLH protein, human
  • Prolactin-Releasing Hormone