Retatrutide molecular structure, formula and mass

Molecular reference data

The mass shown is an average (not monoisotopic) mass computed from the molecular formula using IUPAC standard atomic weights. Mass spectrometers report either average or monoisotopic mass depending on resolution, and the two differ by several daltons at this size.

What the structure means at the bench

• The lipid modification makes the molecule markedly more hydrophobic than a native incretin, which is why it retains strongly on a C18 column and elutes late in a reversed-phase gradient.
• Albumin binding driven by the fatty-diacid chain is the design basis for extended circulating half-life; in a serum-free in-vitro system that binding sink is absent, and effective free concentration differs accordingly.
• At roughly 4.7 kDa, electrospray ionisation produces a multiply-charged envelope rather than a single ion, so identity confirmation works from a deconvoluted mass.
• Amide, methionine and asparagine/glutamine positions are the usual degradation-prone sites in peptides of this class; oxidation and deamidation products are the related substances a purity method is expected to resolve.

Sequence disclosure

Pure Helix does not publish a residue-by-residue sequence for retatrutide. The full sequence is described in the primary characterisation literature and in the corresponding patent filings, and we link to those sources rather than restate a sequence we have not independently verified by sequencing.

Related records

The Molecular Research Index entry for retatrutide carries the same formula and mass alongside the pathway classification, available fill weights and every tested lot. The mechanism and receptor-target pages explain what the molecule does once it is in an assay.

Research use

Pure Helix supplies materials for laboratory research use only. Nothing on this page is medical advice, and none of the material described is for human or veterinary use.