For laboratory research use only · not for human or animal consumption
Peptide Research Reference Laboratory handling & literature
Protocol 02

Storage and stability.

Peptides degrade by a small number of well-understood routes. Storage practice is simply the business of closing each one off.

The four routes of degradation

Nearly all loss of peptide integrity comes down to four mechanisms. Each has a corresponding control, and the controls are the whole of storage practice.

MechanismWhat happensControl
HydrolysisWater cleaves peptide bonds, breaking the chainKeep the material dry. This is the entire reason it ships lyophilised.
OxidationSusceptible residues react with oxygen, altering the moleculeLimit air and light exposure; keep vials sealed and dark.
AggregationMolecules associate and come out of solutionAvoid shaking, foaming and repeated temperature swings.
Microbial growthContaminants multiply in solutionSterile technique; a preserved solvent for multi-entry vials.

Methionine, cysteine and tryptophan are the residues most prone to oxidation. Whether a given compound is vulnerable depends on whether its sequence contains them, which is one practical reason to know the sequence of the material you hold.

Water hydrolysis Oxygen & light oxidation Agitation aggregation Contamination microbial growth Keep it drylyophilised, sealed Keep it darksealed, low light Do not shakeswirl, never foam Sterile techniqueone needle, one entry
Four pathways, four controls. Each route of degradation has a corresponding handling control. Storage practice is little more than closing off all four.

Lyophilised material

In its freeze-dried state a peptide is comparatively robust. Water has been removed, so hydrolysis is largely arrested, and the material tolerates long storage provided it stays dry, cold and dark.

Reconstituted material

Once in solution the material is markedly less stable, because water is now present in quantity and hydrolysis proceeds. Solutions are working stock with a limited life, not a storage format.

Freeze-thaw cycling

Every freeze-thaw cycle stresses the molecule. Ice crystal formation and the concentration changes that accompany freezing both promote aggregation, and the damage accumulates across cycles rather than resetting each time.

Aliquot once, immediately after reconstitution, into single-use volumes. Thawing one small aliquot leaves the rest untouched. Repeatedly thawing and refreezing a single container subjects the entire stock to every cycle.

Quick reference

StateTemperatureLightPractical life
Lyophilised, sealedFrozen, desiccatedDarkLong; the stable format
Lyophilised, short termRefrigeratedDarkShorter, still stable
In solutionRefrigeratedDarkShort; working stock only
In solution, aliquotedFrozenDarkExtended, but thaw each aliquot once only

A note on published stability figures. Specific durations quoted for peptides in solution vary widely between sources and depend on the sequence, the solvent, the pH and the storage temperature. Read any single number as sequence-specific rather than universal, and prefer the supplier's own stability data for the material in hand.