Three main technologies are widely acceptable in protein and peptide separation: reverse phase, ion-exchange, and size exclusion. Diversity of proteins and peptides, and a constant need for better separation of bio-molecules of asimilar structure require new ways of separation.Promixis analternative chromatographytechnology for efficient resolution of peptides and proteins. The technology is based on a combination of two interactions – hydrophobic and ionic. This approach became possible due to a new type of separation media: a chemicalcombination of hydrophobic and ionic functional groupson a ligand bonded to a silica support. With this phase, unparalleled selectivity andpeak capacity can be achieved. Peak capacity of protein digest is significantly higher in this mixed-mode separation compared to either single mode of separation. Similar to traditional ion separation, the buffer concentration plays an important role in the mixed-mode technology altering the degree of ionic interaction of the biomolecules with the stationary phase. The amount of organic modifier is also important in changing the degree of hydrophobic interaction. Independent adjustment of the amount of buffer and organic modifier createsinfinite number of separation conditionsthat are suitable for many types of biomolecules.
SIELC offers several options for Proteins/Peptides:
