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Basics
Lyophilization is the standard procedure for preserving research peptides. The process, the benefits for stability and shelf life — and what this implies for correct storage.
Lyophilization — also known as freeze-drying — is a gentle drying process in which water is removed from a frozen sample through sublimation. This means: the water transitions directly from a solid state (ice) to a gaseous state without passing through the liquid phase.
The process occurs in three phases: freezing the sample, primary drying (sublimation of free water under vacuum), and secondary drying (removal of bound residual water). The result is a dry, porous powder — the lyophilized solid.
Synthetic peptides in aqueous solution are susceptible to hydrolysis, oxidation, and microbial growth. Lyophilization removes water as a reaction medium, thereby drastically slowing down chemical degradation processes.
Advantages compared to liquid formulations:
Important
Lyophilized peptides should be stored at −20°C, protected from light and kept dry. After opening the vial and after reconstitution, different storage conditions apply — use reconstituted solutions at 4°C and promptly.
The following recommendations apply for the optimal stability of lyophilized peptides:
Reconstitution refers to the dissolution of the lyophilized powder in a solvent prior to use in a research context. For research peptides, bacteriostatic water (0.9% benzyl alcohol) or sterile water is typically used.
Bacteriostatic water has the advantage that the benzyl alcohol acts as a preservative, making the reconstituted solution suitable for multiple extractions — in contrast to sterile water without preservatives.
Note
This article is for scientific information purposes only. It does not constitute medical advice. All mentioned products are intended exclusively for research purposes in authorized laboratory environments.