Peptide purification is a process used to separate desired peptides from a mixture of different molecules. This is essential for research and pharmaceutical purposes, as it allows for the extraction of specific peptides for further analysis and applications. Alfa Chemistry offers peptide purification services to customers looking to purify peptides for various research or industrial purposes. We have state-of-the-art equipment and experienced technicians, and master a variety of purification technologies to purify peptides efficiently.
Our Services
Alfa Chemistry provides comprehensive peptide purification services, including but not limited to the following.
- General linear peptide purification
- Routine modified peptide purification
- Specially modified peptide purification
- Drug peptide purification
- Neoantigen peptide purification
- Cosmetic peptide purification
- Stapled peptide purification
- Click peptide purification
- Long peptide purification
- Cyclic peptide purification
- Bicyclic peptide purification
- Glycopeptide purification
- Lipopeptide purification
- Peptoid purification
- Cell-penetrating peptide purification
- Self-assembling peptide purification
- Multiple-antigen peptide (MAP) purification
- Poorly soluble peptide purification
- ...
Purification Technologies
Alfa Chemistry has a number of technologies in the peptide purification and can provide you with various solutions for the peptide purification. Our typical technologies are as follows:
Reverse-phase high-performance liquid chromatography (RP-HPLC)
RP-HPLC is one of the most commonly used methods for peptide purification, which separates peptides based on their hydrophobicity. During RP-HPLC, the peptide sample is applied to a column packed with a stationary phase that has hydrophobic properties, such as C18 silica. The peptides are then eluted from the column using a solvent gradient of increasing organic content, with more hydrophobic peptides being retained longer on the column. The purity and yield of peptides can be optimized by adjusting the gradient slope, flow rate, and column temperature.
Ion exchange chromatography
Ion exchange chromatography separates peptides based on their net charge. In this technique, a stationary phase with charged groups is used to attract peptides with opposite charges. Peptides are loaded onto the column in a buffer solution, and then eluted with a salt gradient or pH gradient. Cation exchange chromatography is used to separate positively charged peptides, while anion exchange chromatography is used to separate negatively charged peptides.
Size exclusion chromatography
Size exclusion chromatography separates peptides based on their molecular size. In this technique, peptides are eluted based on their ability to enter the pores of a stationary phase, with larger peptides eluting first and smaller peptides eluting later. Size exclusion chromatography is often used as a polishing step to remove impurities and aggregates from purified peptide samples.
Affinity chromatography is a chromatographic technique that uses the binding properties of a stationary phase to separate peptides. This technique allows for highly selective purification of peptides based on their binding affinity for the immobilized ligand. Common ligands used in affinity chromatography include antibodies, lectins, and immobilized metal ions.
Solid-phase extraction (SPE)
SPE is a rapid and versatile technique for peptide purification. In this technique, peptides are selectively retained on a solid support, such as a resin or membrane, while unwanted impurities are washed away. The purified peptides can then be eluted from the solid support using a solvent or acid.
