- Document
- CT-01
- Section
- Containers, labels & contamination
- Revised
- Sources checked
- Bands
- −80 °C−20 °C2–8 °C
Container Selection: Glass, Plastic and Peptide Adsorption
Peptides stick to surfaces, and at low concentrations a large share can be lost to the tube wall. How to choose between glass, polypropylene and low-binding plastic, and what closures do.
Bench card
- Adsorption to container walls can remove a large fraction of a dilute peptide solution.
- Losses are worst for hydrophobic or strongly cationic peptides at low concentration.
- Low-binding polypropylene is a good default for dilute solutions; glass suits dry powder and organic solvents.
- Match the tube to the temperature: not every plastic tolerates −80 °C or liquid nitrogen.
- Minimize headspace and choose closures that seal well when cold.
A container does more than hold a sample. Its surface can bind peptide, its walls can let in light or moisture, and its closure decides how much air reaches the contents. For concentrated stocks these effects are small; for dilute working solutions they can dominate the result.
Adsorption: the hidden loss
Peptides adsorb to glass and plastic surfaces through hydrophobic and electrostatic interactions. Because a tube has a fixed surface area, the fraction lost is largest at low concentration. Kristensen and colleagues measured recovery of several peptides from different containers and found losses that, at low concentrations, could reach most of the peptide, with large differences between container materials and between peptides. Goebel-Stengel and colleagues reported similar behaviour for regulatory peptides and showed that the choice of tube and additives changed recovery substantially.
Risk is highest for:
- Hydrophobic or amphipathic sequences.
- Strongly basic (cationic) peptides on glass, whose surface is negatively charged.
- Solutions at low micromolar concentration or below.
- Long contact times and large surface-to-volume ratios.
Comparing materials
| Material | Strengths | Limits |
|---|---|---|
| Borosilicate glass (Type I) | Chemically resistant, impermeable, good for dry powder and organic solvents | Binds cationic peptides; can shed ions at extreme pH |
| Standard polypropylene | Cheap, tough, freezer-safe | Binds hydrophobic peptides |
| Low-binding polypropylene | Reduced adsorption for most peptides | More expensive; performance varies by brand and peptide |
| Polystyrene | Clear, used in plates | Often high binding; poor solvent resistance |
Reducing adsorption
- Keep stock solutions concentrated, typically 1 mg/mL or more, and dilute just before use.
- Use low-binding tubes and tips for dilute working solutions.
- Where the experiment allows, a small amount of organic solvent, acid, or a carrier protein such as albumin can reduce surface loss.
- Minimize transfers: every new surface takes its share.
Temperature and solvent compatibility
Check the manufacturer’s rating before freezing. Most polypropylene microtubes handle −80 °C, but some caps crack or loosen, and only specified cryovials are rated for liquid nitrogen. Solvents such as DMSO, acetonitrile and strong acids can attack some plastics; glass is the safer choice for organic stocks.
Closures and headspace
- Screw caps with an O-ring or a lined cap seal better than snap caps in the freezer.
- Septum-stoppered vials allow withdrawal without opening, but repeated punctures weaken the seal.
- Fill tubes appropriately: a small sample in a large tube has more headspace oxygen and more wall area.
- Use amber or opaque containers, or an opaque box, for light-sensitive material.
References
- Kristensen K, Henriksen JR, Andresen TL. Adsorption of cationic peptides to solid surfaces of glass and plastic. PLoS One. 2015;10(5):e0122419. DOI
- Goebel-Stengel M, Stengel A, Taché Y, Reeve JR Jr. The importance of using the optimal plasticware and glassware in studies involving peptides. Anal Biochem. 2011;414(1):38–46. DOI
- USP General Chapters <660> Containers—Glass and <671> Containers—Performance Testing (including light transmission). United States Pharmacopeia.
- Kerwin BA, Remmele RL Jr. Protect from light: photodegradation and protein biologics. J Pharm Sci. 2007;96(6):1468–1479. DOI