Growth hormone secretagogues · Reference

Sermorelin

Synthetic 29-residue N-terminal fragment of human GHRH · Also known as GHRH(1-29)-NH2, GRF(1-29), Geref

Sermorelin is the synthetic 29-residue N-terminal fragment of human GHRH — the minimum sequence that still binds and activates the GHRH receptor. Its analytical profile is a textbook case of methionine oxidation and aspartimide chemistry on a moderately long backbone.

Chemistry at a glance

CAS
86168-78-7
Formula
C149H246N44O42S
Avg. MW
3357.88 Da
Monoisotopic
Not published — confirmed per batch by LC-HRMS
Sequence
YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH2

Chemistry summary only. CertikLabs does not publish dosing, administration, or clinical guidance for any peptide.

Structure and chemistry

Sermorelin is a linear 29-residue peptide with sequence YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH2 — the first 29 residues of human growth-hormone-releasing hormone, terminated as the C-terminal amide. Molecular formula C149H246N44O42S, average mass approximately 3357.88 Da. CAS registry: 86168-78-7.

The 29-mer is the minimum fragment that retains full intrinsic GHRH-receptor agonist activity; the 30+ residues of the native 44-mer contribute primarily to half-life and tissue distribution. Sermorelin therefore has a much shorter plasma half-life than long-acting GHRH analogs such as CJC-1295.

Synthesis and where impurities come from

Sermorelin is produced by Fmoc solid-phase peptide synthesis on a Rink-amide-style resin (to deliver the C-terminal amide). The main impurity sources are:

  • Methionine oxidation at position 27. The single Met residue is highly susceptible to oxidation during synthesis, storage, and reconstitution; sulfoxide (+16 Da) and sulfone (+32 Da) variants are routine.
  • Aspartimide and deamidation. The Asp-Met segment is a textbook aspartimide-formation site under repeated piperidine deprotection. Asn8 deamidates over storage to a mixture of α- and β-Asp.
  • C-terminal truncations. Loss of the terminal Arg-NH2 produces des-Arg29 — a -156 Da analyte that is easy to confuse with the main product by intact mass alone if mass accuracy is poor.
  • Loss of the C-terminal amide. Over-acidic cleavage hydrolyzes the amide to the free acid (-1 Da).

See common peptide impurities for the broader taxonomy.

How CertikLabs verifies sermorelin

The standard CertikLabs panel for a sermorelin batch:

  • RP-HPLC purity (C18, 0.1% TFA / MeCN, UV 214 nm)
  • LC-HRMS identity (ESI-Q-TOF, deconvoluted average mass against C149H246N44O42S)
  • Tryptic peptide mapping with LC-MS/MS for sequence confirmation
  • Quantitative AAA for content
  • Met-oxidation screen by extracted-ion chromatograms (Δ+16, +32 Da)

Each method, including column, mobile phase, gradient, and detection conditions, is reported on the Certificate of Analysis so the result is reproducible. See how to read a peptide COA for what each section should contain.

Published mechanism (literature summary)

Agonist at the GHRH receptor on pituitary somatotrophs, stimulating pulsatile growth-hormone release. Pharmacology is well established in the published GHRH literature.

Primary sources:

CertikLabs does not publish dosing, administration routes, or clinical recommendations for sermorelin.

Stability and storage (chemistry only)

Lyophilized sermorelin is generally stable refrigerated and protected from light. Reconstituted material is sensitive to Met(27) oxidation, deamidation at Asn/Gln, and aspartimide formation; pH, container, and oxygen exposure all influence stability and any working solution should be re-verified analytically.

Frequently asked questions

What is sermorelin?

Sermorelin (CAS 86168-78-7) is the synthetic 29-residue N-terminal fragment of human growth-hormone-releasing hormone (GHRH), supplied as the C-terminal amide (GHRH(1-29)-NH2). Molecular formula C149H246N44O42S, average mass approximately 3357.88 Da. The 29-mer retains the full intrinsic GHRH-receptor agonist activity of the 44-residue native hormone.

How is sermorelin purity tested?

Purity is measured by reverse-phase HPLC on a C18 column with a 0.1% TFA / acetonitrile gradient and UV detection at 214 nm. Identity is confirmed by LC-HRMS against the theoretical deconvoluted average mass for C149H246N44O42S, and tryptic peptide mapping with LC-MS/MS confirms full sequence coverage.

What are the most common sermorelin impurities?

C-terminal truncations (especially loss of the terminal Arg-NH2), Met(27) oxidation to sulfoxide and sulfone, deamidation at Asn8 and Gln residues, aspartimide formation at Asp-Met and Asp-Lys segments, loss of the C-terminal amide (free-acid impurity), and residual TFA or acetate counter-ion. A well-designed analytical panel resolves all of these from the main peak.

How can I verify a sermorelin Certificate of Analysis?

An independent CertikLabs Certificate of Analysis is content-hashed (SHA-256) and anchored on a public blockchain at issuance. Anyone holding the report can recompute the hash and confirm it matches the on-chain record — the document is tamper-evident without trusting any single party.

Published 2026-05-16