Five Residues, Three Oddballs: The Anatomy of Ipamorelin

Ipamorelin looks tiny on paper: Aib-His-D-2Nal-D-Phe-Lys-NH2. But look closer and only two of those five building blocks, His and Lys, are normal. The rest are the interesting part.

Aib: the stiff one

Aib stands for alpha-aminoisobutyric acid. It carries two methyl groups on its alpha carbon, which crowds the backbone and locks the angle. Aib at the front also makes the peptide harder for enzymes to recognize.

D-2-naphthylalanine: the bulky one

This residue is right-handed and has a large two-ring side chain. Bulk and handedness together make it a good fit for its receptor pocket and a poor fit for enzymes.

D-phenylalanine: the mirror

Right next door sits another D residue. Two D-amino acids in a row is a deliberate design from the 1990s work that followed Cyril Bowers’ growth hormone releasing peptides.

The finish

The chain ends in an amide instead of a free acid, removing a negative charge. The net result is a molecule of about 712 Da that behaves nothing like a natural peptide.

It is one of two components in our CJC-1295 No DAC + IPA 10mg listing. Keep reading, because the next time you see a name like this, you will know to ask which residues are unusual.

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For laboratory research use only. Not for human or veterinary use, and not intended to diagnose, treat, cure or prevent any condition. This article is educational and is not medical advice.