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How to store peptides?
For long term storage of peptides, we recommend storing peptides as a solid powder, as peptides in the raw powder state can be stored at -20 °C or lower to minimise degradation. We also recommend that custom peptides are rechecked for purity every 2 years.
2. Peptides in solution Peptides in solution are less stable and prone to degradation. Aqueous solutions used to dissolve peptides should be sterile and pure. In solution, a certain amount of peptide may be degraded, depending on the amino acids present in the sequence.
A few examples are shown below:
- Peptides containing methionine, cysteine or tryptophan residues should have a limited storage time in solution due to oxidation. These peptides should be dissolved in an oxygen-free solvent.
- Glutamine and asparagine can be deamidated to glutamic acid and aspartic acid, respectively. - Cysteine can undergo oxidative cyclisation to form Cys-Cys disulphide bonds (either intra- or inter-disulphide bonds can be formed).
- Charged residues (Asp, Glu, Lys, Arg, His) are hygroscopic (absorbing water from moisture in the air) and can easily form a viscous, clear oil, a physical change that may not affect the properties of the peptide.
It is recommended that such peptides are first lyophilised to remove traces of water, degassed with nitrogen to ensure that there is no water vapour in the vial, and then quickly capped.
To prevent damage from repeated freeze-thaw cycles, we recommend that users only dissolve the amount of peptide required for the current experiment. Any excess solution should be stored at ≥ -20 °C until needed.
Avoid humidity As humidity can greatly reduce the long-term stability of peptides, we recommend that peptides should be equilibrated to room temperature in a desiccator before opening vials. After peptide dispensing, the remaining peptide in the tube should be gently purged with anhydrous nitrogen, the container capped, sealed with a sealing film, and stored at -20 °C.
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Lyophilised Peptides
For long-term storage of peptides, we recommend storing peptides as a solid powder. Lyophilised peptides can be stored at -20 °C or lower with little degradation. Customers are advised to recheck their customised peptides every 2 years from the date of QC release.
Peptides in solution
Peptides in solution are much less stable and are susceptible to degradation. Solutions of water used to dissolve peptides should be sterile and purified.
In solution, some amount of the peptide may degrade depending on the amino acids present in the sequence. A few examples of which are shown below:
- Peptides containing methionine, cysteine, or tryptophan residues should have limited storage time in solution due to oxidation. These peptides should be dissolved in oxygen-free solvents.
- Glutamine and asparagine can deamidate to Glu and Asp, respectively.
- Cysteines can undergo oxidative cyclization to form Cys-Cys disulfide bridges (intra or inter disulfide bridges can form).
- Charged residues (Asp, Glu, Lys, Arg, His) are hygroscopic (take up water from moisture in the air) and will easily form a viscous clear oil. This physical change may not affect the properties of the peptide. It is recommended that such peptides be first lyophilized to remove trace amounts of water, degassed with N2 to ensure that there is no water vapor in the vial, and quickly capped.
To prevent any damage caused by repeated freeze-thaw cycles, we recommend that the user only dissolves the amount of peptide needed for the immediate experiment. Any excess solutions should be stored at ≥ -20 oC until needed.
Avoid moisture
As moisture will greatly reduce the long-term stability of peptides, we recommend that the peptide should be allowed to equilibrate to room temperature in a desiccator before opening the vial. Once the peptide has been dispensed, any remaining peptide in the tube should be gently purged with anhydrous nitrogen, the container recapped, sealed with parafilm, and stored at -20 °C.
The solubility characteristics of different peptides vary greatly. Residues such as Ala, Cys, Ile, Leu, Met, Phe and Val increase the chances of peptide hydrophobicity and solubility in aqueous solution, and it is recommended that customers adhere to the following guidelines when customising their peptides.
Solubility properties
Peptide solubility is highly dependent on the amino acid sequence. Hydrophobic peptides (high propensity of A, F, G, V, L, I, M, W, P) in nature, will require an organic solvent to dissolve. Acidic peptides (high propensity of D, E in the peptide sequence) require a basic aqueous buffer to dissolve, while basic peptides (high propensity of K, H, and R) require an acidic aqueous buffer to dissolve.
Selection of solvent
Taking into consideration the limitations of your assay, we recommend that the following guideline be used to determine the best solvent to dissolve your peptide
Hydrophobic peptides
To reconstitute a hydrophobic peptide, add 100 µL of DMSO and sonicate until a homogenous solution forms. Next, add your buffer of choice to form a 1 mg/mL solution (a higher concentration of peptide will require a greater amount of DMSO).
Hydrophilic (acidic) peptide
To reconstitute an acidic peptide, add 100 µL of 1% NH4OH to 1 mg of the peptide and vortex. After the formation of a clear solution, add your buffer of choice to form a 1 mg / mL solution.
Hydrophilic (basic) peptide
To reconstitute a basic peptide, add distilled water to the 1 mg of peptide and vortex.
Use and storage
Reconstituted peptides can be stored frozen at -20°C for a short time, but it is advisable to prepare multiple aliquots to avoid multiple freeze-thaw cycles. We recommend that all aliquoted solutions be lyophilized if the peptide is going to be stored for extended periods at -20 oC.
Peptides with a propensity to aggregate
For peptides that tend to aggregate due to the presence of multiple Cysteines, we recommend that these peptides be dissolved in degassed solutions and/or acidic conditions.
Additionally, some types of peptides have a propensity to form secondary and tertiary structures once dissolved. We recommend that these peptides be first dissolved in solvents such as HFIP (hexafluoroisopropanol) and then evaporated using a stream of nitrogen. The HFIP helps to break up the hydrogen bonding network that aids in forming the secondary and tertiary structures.
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