PHG · REV 2026.10 For laboratory research use only. Not medical or dosing guidance.
Peptide Handling Guide Storage, handling and documentation for research peptides
Document
CS-IPAMOR
Type
Compound handling sheet
Revised
Sources checked
Bands
−20 °C

Ipamorelin Handling Sheet

Also known as NNC 26-0161

A five-residue synthetic peptide containing non-natural amino acids (Aib, D-2-naphthylalanine, D-phenylalanine) and a C-terminal amide. Standard storage applies, with light protection for its aromatic groups.

1 min read

Identity

Sequence
Aib-His-D-2Nal-D-Phe-Lys-NH2
Formula
C38H49N9O5
Molecular weight
711.9 g/mol (average)
Usual supplied form
Lyophilized powder, often as acetate salt
Record
PubChem

Formula and weight are for the free peptide. Salt forms (acetate, TFA) weigh more; use the figure on the lot's COA.

Storage & sensitivity

Lyophilized−20 °C
In solution−20 °C
Oxidation
Moderate
Light
Moderate
Moisture
Moderate
Inferred from structure

Little compound-specific stability data is published. Guidance follows from the sequence and general peptide chemistry.

Bench card

  • Non-natural residues make it more resistant to enzymes, but do not prevent chemical degradation.
  • Naphthylalanine and phenylalanine absorb UV; protect solutions from light.
  • His2 can oxidize in the presence of metals or light.
  • Basic (Lys, His, N-terminal amine); dissolves in water or dilute acetic acid.
  • Mass spectrometry confirms composition, but D/L configuration needs chiral analysis.

Handling-relevant features

FeatureWhy it matters for handling
Aib1 (α-aminoisobutyric acid)Non-natural residue that restricts backbone flexibility and resists peptidases
His2Metal-catalyzed and photosensitized oxidation site
D-2Nal3 (D-2-naphthylalanine)Large aromatic group; UV absorber and hydrophobic
D-Phe4Aromatic; D-configuration adds protease resistance
Lys5-NH2C-terminal amide removes the negative C-terminal charge

What it is

Ipamorelin is a synthetic pentapeptide, Aib-His-D-2Nal-D-Phe-Lys-NH2, described by Raun and colleagues in 1998. Three of its five residues are non-natural or D-configured.

Stability profile

The unusual residues were chosen for biological stability: they make the peptide a poor substrate for many peptidases. Chemical stability is a separate matter. The naphthylalanine and phenylalanine side chains absorb ultraviolet light, and histidine is a known oxidation site, so light and oxygen remain the main storage concerns. There are no Asn, Gln or Asp residues to deamidate or isomerize.

Storage

Form Recommended Notes
Sealed powder −20 °C Desiccant; opaque box
Solution, days 2–8 °C Amber tube
Solution, longer −20 °C Single-use aliquots

Analytical notes

Expected [M+H]+ is about m/z 712.9 (average). Because the structure depends on D-amino acids, a correct mass does not confirm the correct stereochemistry; chiral analysis is needed for that.

References

  1. Raun K, Hansen BS, Johansen NL, et al. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998;139(5):552–561. DOI
  2. Kerwin BA, Remmele RL Jr. Protect from light: photodegradation and protein biologics. J Pharm Sci. 2007;96(6):1468–1479. DOI
  3. Li S, Schöneich C, Borchardt RT. Chemical instability of protein pharmaceuticals: mechanisms of oxidation and strategies for stabilization. Biotechnol Bioeng. 1995;48(5):490–500. DOI
  4. Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharm Res. 2010;27(4):544–575. DOI

This sheet covers laboratory storage and handling of research material only. It does not describe use in humans or animals, and the supplier's datasheet for your lot takes priority.