Growth hormone secretagogues: characterization, efficacy, and minimal bioactive conformation

Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):11165-9. doi: 10.1073/pnas.92.24.11165.


Another class of growth hormone (GH) secretagogues has been discovered by altering the backbone structure of a flexible linear GH-releasing peptide (GHRP). In vitro and in vivo characterization confirms these GH secretagogues as the most potent and smallest (M(r) < 500) reported. Anabolic efficacy is demonstrated in rodents with intermittent delivery. A convergent model of the bioactive conformation of GHRPs is developed and is supported by the NMR structure of a highly potent cyclic analog of GHRP-2. The model and functional data provide a logical framework for the further design of low-molecular weight secretagogues and illustrate the utility of an interdisciplinary approach to elucidating potential bound-state conformations of flexible peptide ligands.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Consensus Sequence
  • Female
  • Growth Hormone / metabolism*
  • Hormones / chemistry*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Oligopeptides / chemistry*
  • Peptides, Cyclic / chemistry*
  • Pituitary Gland, Anterior / metabolism
  • Protein Structure, Secondary
  • Rats
  • Rats, Sprague-Dawley
  • Secretory Rate
  • Structure-Activity Relationship


  • Hormones
  • Oligopeptides
  • Peptides, Cyclic
  • Growth Hormone
  • growth hormone-releasing peptide-2