Sermorelin
A synthetic 29-residue C-terminally amidated peptide corresponding to the N-terminal fragment of a 44-residue hypothalamic peptide.
Molecular Profile
- Type
- Synthetic peptide (29 residues, C-terminal amide)
- Molecular formula
- C149H246N44O42S
- Molecular weight
- ~3,358 g/mol
- CAS number
- 86168-78-7
- Amino acids
- 29
- Sequence
- Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2
- Modification
- C-terminal amidation; sequence corresponds to residues 1-29 of human GHRH (the N-terminal fragment that retains intrinsic activity).
Mechanism & Target Class
A synthetic 29-residue C-terminally amidated peptide corresponding to the N-terminal fragment (residues 1-29) of a 44-residue hypothalamic peptide - the minimal segment that retains the intrinsic structural activity of the longer parent. Solution NMR in a membrane-mimetic solvent describes substantial alpha-helical character, and cryo-EM of the peptide bound to its class B1 (secretin-like) G-protein-coupled receptor complex resolves a continuous alpha-helical conformation contacting the receptor extracellular domain, extracellular loops, and transmembrane helices. Binding is described by a two-domain ('two-step') model in which the peptide engages both the receptor extracellular domain and its transmembrane core. As a small unmodified peptide it carries a single oxidation-sensitive methionine and is characterized by rapid circulatory clearance, distinguishing it from chemically stabilized analogs bearing acyl or amino-acid-substitution modifications.
Storage & Handling
- Lyophilized
- -20°C (-80°C long term); powder protected from light, typically stable many months desiccated.
- Handling
- Avoid freeze-thaw; aliquot; protect from light and moisture. Contains an oxidation-sensitive methionine.
Primary Database
References (20)
Reviews
1Granata R, et al. (2025). Nat Rev Endocrinol
- 2
Montero-Hidalgo AJ, et al. (2025). Rev Endocr Metab Disord
- 3
Walker RF. (2006). Clin Interv Aging
- 4
Lin-Su K, Wajnrajch MP. (2002). Rev Endocr Metab Disord
- 5
Prakash A, Goa KL. (1999). BioDrugs
Clinical
6Baker LD, et al. (2012). Arch Neurol
- 7
Khorram O, et al. (1997). J Clin Endocrinol Metab
- 8
Vittone J, et al. (1997). Metabolism
- 9
Thorner M, et al. (1996). J Clin Endocrinol Metab
- 10
Corpas E, et al. (1992). J Clin Endocrinol Metab
- 11
ClinicalTrials.gov. ClinicalTrials.gov
Primary research
12Zhou F, et al. (2020). Nat Commun
- 13
Kanashiro-Takeuchi RM, et al. (2012). Proc Natl Acad Sci USA
- 14
Kanashiro-Takeuchi RM, et al. (2010). Proc Natl Acad Sci USA
- 15
Godfrey P, et al. (1993). Nat Genet
- 16
Mayo KE. (1992). Mol Endocrinol
- 17
Theriault Y, et al. (1988). Biopolymers
- 18
Ling N, et al. (1984). Proc Natl Acad Sci USA
- 19
Rivier J, et al. (1982). Nature
- 20
Guillemin R, et al. (1982). Science
