Details up front: cagrilintide · 2–8 °C.
I can find plenty of assertions about this and almost no reasoning, which is usually a sign that nobody has checked.
Assume no laboratory access beyond what I can pay a third party for.
Which parts of this are load-bearing and which parts are habit?
Whatever the refrigerated figure is, divide it by about 1. 2–8 °C is the condition the rule of thumb is anchored to, so it is the baseline rather than a multiplier: everything else in this thread is quoted relative to it. So a preparation with a twenty-eight day refrigerated figure has roughly 28 days at 2–8 °C on the same assumption — an order-of-magnitude answer, not a shelf life, and it says nothing about sterility, which has its own clock. "Within specification" also needs a specification: purity, content, or both, and at what limit. Without that the question has no numerical answer at all.
The relevant point is that a mass shift of plus one dalton is deamidation and plus sixteen is oxidation, so degradation is often visible in a mass spectrum if anyone looks.
Adsorption onto glass and plastic is significant at low concentrations — micrograms per millilitre — and negligible at milligrams per millilitre. It is the usual explanation for an apparent loss in a dilute preparation.
| Pathway | Dominant when | Detected by |
|---|---|---|
| Deamidation | Solution, neutral to alkaline pH | RP-HPLC, +1 Da on MS |
| Oxidation | Light, trace metals, peroxides | RP-HPLC, +16 Da on MS |
| Hydrolysis | Solution, extremes of pH | RP-HPLC, fragment masses |
| Aggregation | Agitation, interfaces, high concentration | SEC, visual haze; often invisible on RP-HPLC |
| Freeze-concentration damage | Freeze-thaw of buffered solution | SEC, loss of recovered content |
Hydrolysis cleaves the backbone, most readily at aspartate-proline and aspartate-glycine sequences, and is acid-catalysed. In a dry solid it barely proceeds at all.
Deamidation via the succinimide intermediate is well characterised, with sequence-dependent rates highest for asparagine-glycine motifs.
The caveat is that none of these pathways can be seen by looking at a vial, and a clear solution can be substantially degraded.
At dilute concentrations, suspect adsorption before you suspect chemistry.
Analytical standards and reagents with traceable certificates. Every quantitative result you read inherits the accuracy of the standard behind it.
Shop standardsOn the detail: this is answerable from the chemistry rather than from anecdote, which is unusual and welcome.
Light exposure matters for tryptophan-containing sequences and for anything with a chromophore. Amber vials and a closed box are free mitigations.
A mass spectrum resolves most of this: minus eighteen is dehydration or succinimide, plus one is deamidation, plus sixteen is oxidation, and an unchanged mass with a shifted retention time is an isomer.
Aggregation at air-liquid interfaces is established from surface-tension and particle-count studies and is the basis for anti-agitation handling guidance.
Sequence determines which pathways apply, so general statements are general.
Swirl, never shake. Aggregation is a handling problem more than a time problem.
Answer first: the degradation pathways worth knowing are hydrolysis, deamidation, oxidation, aggregation and adsorption, and each has a different trigger and a different mitigation.
Deamidation converts asparagine or glutamine to the corresponding acid via a succinimide intermediate, adding one dalton. It is base-catalysed, accelerates above neutral pH and is the dominant aqueous pathway for many peptides.
On the detail: oxidation targets methionine, cysteine and tryptophan, adding sixteen daltons per oxygen. It is catalysed by trace metals and promoted by dissolved oxygen and by light.
Metal-catalysed oxidation of methionine is documented across peptide and protein formulations and is why chelators appear in some formulations.
Cold, dry, dark, still. Those four words cover most of the mitigation.
The relevant detail is that aggregation is a physical process and is the one most often caused by handling rather than by time.
Aggregation is physical: peptides unfold at air-liquid interfaces and associate. Shaking maximises that interface, which is why swirling and shaking produce visibly different outcomes on the same vial.
Adsorption losses at low concentrations are quantified in formulation studies and are the reason carrier proteins are used in dilute preparations.
A mass spectrum names the pathway. Plus one, plus sixteen, minus eighteen.
edited 30 Jun 2026 by coldpack_88 — added the method parameters
The short version: water enables most of it, oxygen enables oxidation, surfaces enable adsorption, and agitation enables aggregation.
Freeze-thaw cycling drives aggregation through concentration at the ice interface and pH shifts as buffer components crystallise out at different rates. Each cycle costs something.
Deamidation kinetics for asparagine in peptides are well characterised and strongly sequence-dependent: the residue following the asparagine dominates the rate, with glycine and serine at the n+1 position accelerating it by an order of magnitude relative to bulkier residues. That is why two peptides in the same buffer at the same temperature can have quite different shelf lives.
Apparent loss in a dilute preparation is usually adsorption rather than degradation and is worth ruling out first.
Sequence decides which pathways are even available. Check the residues.
Ask PeptideStack is a static archive. Posting is closed, but the norms are worth stating: answer the question that was asked, show your working, cite the trial or the certificate, and say plainly where the evidence runs out.