Structure-activity studies on prolactin-releasing peptide (PrRP). Analogues of PrRP-(19-31)-peptide.
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.
Boyle
Robert G
RG
Millennium Pharmaceuticals Limited, Granta Park, Great Abingdon, Cambridge CB1 6ET, UK.
Downham
Robert
R
Ganguly
Tanmoy
T
Humphries
John
J
Smith
Jeff
J
Travers
Stuart
S
D000595:Amino Acid Sequence; D020013:Calcium Signaling / Q000187:drug effects; D002460:Cell Line; D003500:Cyclization; D004220:Disulfides / Q000737:chemistry; D006801:Humans; D007028:Hypothalamic Hormones / Q000737:chemistry* / Q000494:pharmacology*; D020128:Inhibitory Concentration 50; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry* / Q000494:pharmacology*; D056690:Prolactin-Releasing Hormone; D013329:Structure-Activity Relationship
D004220:Disulfides; D007028:Hypothalamic Hormones; D009479:Neuropeptides; C534377:PRLH protein, human; D056690:Prolactin-Releasing Hormone