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Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC)
Isocratic Separation and Selective Isolation of Charged Solutes
ERLIC is an innovative chromatography method that enables isocratic separations that would typically require gradients. It’s particularly effective for selectively isolating highly charged solutes, such as phosphopeptides, from complex mixtures. ERLIC combines ion-exchange with hydrophilic interaction, allowing for precise control of solute retention. This dual mechanism ensures high-resolution separations even for solutes with multiple negative charges, such as peptides with post-translational modifications (PTMs).
In ERLIC, the column’s charge is matched to the sample solutes, and hydrophilic interaction retains the solutes on the column despite electrostatic repulsion. The specific pH of the mobile phase ensures that solutes maintain a charge that interacts favorably with the stationary phase, enabling selective separation of charged molecules like phosphopeptides.
In ERLIC, the negative charges on the peptide’s C-terminus and modification sites (e.g., phosphate or sialic acid groups) interact with the stationary phase to enhance retention. This slows the elution of peptides with multiple negative charges, providing a highly selective method for isolating peptides with post-translational modifications.
PolyLC ERLIC Columns: Optimized for Separation of Charged Solutes
- Cation-exchange (PolySULFOETHYL A™ or PolyCAT A™): Ideal for the isolation of negatively charged solutes like nucleotides or acidic peptides.
- Anion-exchange (PolyWAX LP™): Designed for the selective isolation of phosphopeptides, glycopeptides, and other peptides with multiple negative charges.
The example above illustrates the selectivity of ERLIC over HILIC as it is able to separate phosphopeptides of the same charge, and selectively isolate them based on the PTM location.
This example shows the separation of nucleotides on PolySULFOETHYL A™. Normally the NTP’s elute much later than the NMP’s and NDP’s in either the anion-exchange or HILIC mode. In ERLIC they elute isocratically in the same time frame as the other nucleotides.
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Selective Isolation of Phosphopeptides in a Tryptic Protein Digest
ERLIC is well suited for the high resolution of samples containing thousands of phosphopeptides.
Learn how the ERLIC method enabled efficient chromatographic separation of phosphorylated peptides from nonphosphorylated peptides and separation of phosphopeptides with different phosphorylation states in a tryptic digest of HeLa proteins.
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Learn More About ERLIC
Dive deeper into the principles and applications of ERLIC with these key publications. Explore the foundational research and advancements in orientation effects.
Original Publication on ERLIC: discover the groundbreaking research that introduced the ERLIC technique and its applications.
Orientation Effects of ERLIC: gain insights into how orientation impacts the performance of ERLIC in the separation of proteolytic peptides.
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