Ball-and-stick amino acid backbone with a teal-highlighted N-terminal cap group, illustrating tesamorelin sequence and N-terminal modification stability.
Mindful Research

Tesamorelin Peptide: Sequence, N-terminal Modification and Stability

By: Mindful Research Team2 min read

Key takeaways

  • The sequence is human GHRH(1-44)-NH2 with a trans-3-hexenoyl cap on Tyr1.
  • The cap adds about 96.1 Da and blocks the free N-terminal amine that dipeptidyl peptidase IV needs.
  • Met27 oxidation (+16 Da) and Asn/Gln deamidation (+0.98 Da) are the main solution liabilities.
  • Track stability by RP-HPLC time courses confirmed with LC-MS in the real assay buffer.
  • For in vitro research use only.

The tesamorelin peptide is the 44-residue human GHRH sequence, YADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQERGARARL-NH2, carrying a trans-3-hexenoyl group on the N-terminal tyrosine. This guide covers the sequence, what the N-terminal modification changes chemically, and which positions limit stability in solution. It builds on the overview in the tesamorelin structure and in-vitro research profile.

What is the tesamorelin sequence?

Residues Sequence
1-10 YADAIFTNSY
11-20 RKVLGQLSAR
21-30 KLLQDIMSRQ
31-40 QGESNQERGA
41-44 RARL-NH2

The parent peptide has the formula C221H366N72O67S and an average mass near 5135.9 g/mol. The Tesamorelin listing carries the acetate-form figures, C223H370N72O69S and 5195.908 g/mol, the difference being one acetic acid (60.05 Da).

What does the trans-3-hexenoyl group change?

The modification is an N-acyl cap: a six-carbon unsaturated acyl group joined to the alpha-amine of Tyr1. It adds about 96.1 Da (C6H8O) to the peptide and removes the free N-terminal amine. Native GHRH is cleaved after residue 2 by dipeptidyl peptidase IV, which requires that free amine; capping it reduces that cleavage in peptidase-containing media, which is the reason the analog is used for longer incubations.

Which positions limit stability in solution?

Liability Position Mass change How it is detected
Methionine oxidation Met27 +16 Da (sulfoxide) LC-MS; earlier RP-HPLC elution
Deamidation Asn8, Asn35, Gln residues +0.98 Da High-resolution MS; shifted HPLC peak
Adsorption and aggregation Whole 44-mer, high concentration None Loss of recovery from low-bind versus standard plastic

Because the peptide is long and contains an oxidation-prone methionine, lyophilized storage is the default; the basics are explained in what freeze-dried means for peptides.

How is stability checked in the laboratory?

  • Run a stability-indicating RP-HPLC gradient and track the main-peak area over time points at 4 C and 37 C in the actual assay buffer.
  • Confirm any new peak by LC-MS: +16 Da points to oxidation, +1 Da to deamidation, and a loss of about 96 Da to loss of the hexenoyl cap.
  • Use low-bind tubes and single-use aliquots, and record the number of freeze-thaw cycles.

The identity checks referred to above are expanded in confirming tesamorelin identity by CAS and mass spectrometry.

Related research guides

Research-use note

All materials discussed are supplied for in vitro laboratory research use only, and are not for human or animal use.

Frequently asked questions

What is the tesamorelin peptide sequence?

Tesamorelin is human GHRH(1-44)-NH2, YADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQERGARARL-NH2, with a trans-3-hexenoyl group on the N-terminal tyrosine. View Tesamorelin

What does the N-terminal modification do?

It caps the free N-terminal amine with a trans-3-hexenoyl group (+96.1 Da), reducing dipeptidyl peptidase IV cleavage and extending activity in peptidase-containing media.

Which residues limit stability in solution?

Met27 is prone to oxidation (+16 Da), and Asn and Gln residues can deamidate (+0.98 Da); both are detected by LC-MS. Lyophilized peptide basics

How is stability measured?

By stability-indicating RP-HPLC over time points in the actual assay buffer, with new peaks identified by LC-MS. Tesamorelin research profile

Is it for human or animal use?

No. It is supplied for in vitro laboratory research use only.