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Peptide Purification

Methods and techniques for peptide purification including HPLC, size exclusion, and ion exchange chromatography.

12 min readOctober 5, 2025BioInfinity Lab

Research Use Only: All products on this site are for Research and Development use only. Products are not intended for human consumption. The statements made within this website have not been evaluated by the US Food and Drug Administration.

The Importance of Peptide Purification

Peptide purification is essential for obtaining research-grade materials. After synthesis, crude peptides typically contain impurities including deletion sequences, truncated products, and protecting group remnants. Purification removes these contaminants to achieve the high purity levels required for meaningful research.

High-Performance Liquid Chromatography (HPLC)

HPLC is the gold standard for peptide purification. This technique separates molecules based on their interactions with a stationary phase (column) and mobile phase (solvent).

Reverse-Phase HPLC (RP-HPLC)

The most common method for peptide purification, RP-HPLC uses:

  • Stationary phase: Hydrophobic silica (typically C18 or C8)
  • Mobile phase: Water/acetonitrile gradient with TFA modifier
  • Separation principle: Hydrophobic interactions

Peptides elute based on hydrophobicity—more hydrophobic peptides require higher organic solvent concentrations.

HPLC Parameters

  • Column selection: Pore size (100-300 Å) and particle size affect resolution
  • Gradient optimization: Shallow gradients improve separation of similar species
  • Flow rate: Affects peak resolution and run time
  • Detection: UV absorbance at 214-220 nm (peptide bond) or 280 nm (aromatic residues)

Ion Exchange Chromatography

This technique separates peptides based on charge:

  • Cation exchange: Retains positively charged peptides
  • Anion exchange: Retains negatively charged peptides

Peptides are eluted by increasing salt concentration or changing pH. Ion exchange is particularly useful for separating peptides with similar hydrophobicity but different charges.

Size Exclusion Chromatography (SEC)

Also called gel filtration, SEC separates molecules by size:

  • Large molecules elute first (excluded from pores)
  • Small molecules elute later (can enter pores)
  • Useful for removing small molecule impurities or buffer exchange

Purity Assessment

After purification, purity is verified using analytical methods:

Analytical HPLC

A single, sharp peak indicates high purity. The area percentage of the main peak relative to total peak area gives purity estimation.

Mass Spectrometry

Confirms the molecular weight matches the expected mass, verifying identity and detecting modifications.

Amino Acid Analysis

Quantifies amino acid composition to confirm sequence and assess purity.

Purity Grades

Research peptides are typically offered at different purity levels:

  • >95% purity: Suitable for many research applications
  • >98% purity: Higher quality for sensitive assays
  • ≥99% purity: Premium grade for the most demanding applications

Factors Affecting Purification

  • Peptide length: Longer peptides are more challenging to purify
  • Hydrophobicity: Very hydrophobic peptides may aggregate
  • Modifications: Post-translational modifications affect behavior
  • Scale: Large-scale purification requires process optimization

Quality Documentation

Reputable suppliers provide Certificates of Analysis (COA) documenting:

  • HPLC chromatogram showing purity
  • Mass spectrometry data confirming identity
  • Batch-specific purity percentage
  • Storage and handling recommendations

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Disclaimer: These Peptides are for Research use Only and not intended for Human Use. The information provided in this article is for educational purposes only and should not be construed as medical advice.