A modified 5-amino-acid ghrelin fragment ([Trp3,Arg5]-ghrelin 1-5) retained full GH-releasing and appetite-stimulating activity through the GHS receptor, demonstrating the extreme minimal pharmacophore for ghrelin function.
Key finding[Trp3,Arg5]-ghrelin(1-5), a modified pentapeptide, stimulated both GH secretion and food intake through GHS-R — demonstrating that ghrelin's full biol
What the researchers found
[Trp3,Arg5]-ghrelin(1-5), a modified pentapeptide, stimulated both GH secretion and food intake through GHS-R — demonstrating that ghrelin's full biological activity can be captured in just 5 amino acids with appropriate modifications.
Why it matters
Relevant for ghrp, hormone-optimization, peptide-design.
How the study worked
animal-study study on ghrp, hormone-optimization.
What this study cannot tell us
See abstract.
How to read the evidence
preliminary evidence.
When this study was published
Published in 2006.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
[Trp3, Arg5]-ghrelin(1-5) stimulates growth hormone secretion and food intake via growth hormone secretagogue (GHS) receptor.
Peptides, 27(7), 1632-7
Citation
Ohinata, Kousaku; Kobayashi, Kanako; Yoshikawa, Masaaki. (2006). [Trp3, Arg5]-ghrelin(1-5) stimulates growth hormone secretion and food intake via growth hormone secretagogue (GHS) receptor.. Peptides, 27(7), 1632-7.