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Related Experiment Videos

Peptides as affinity surfaces for protein purification

A Pingali1, B McGuinness, H Keshishian

  • 1PerSeptive Biosystems, Framingham, MA-01701, USA.

Journal of Molecular Recognition : JMR
|September 1, 1996
PubMed
Summary

Researchers developed novel affinity chromatography media by synthesizing peptides directly onto POROS resin. This method efficiently captures fibrinogen and albumin, demonstrating its potential for protein purification under non-denaturing conditions.

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Area of Science:

  • Biochemistry
  • Chromatography
  • Protein Purification

Background:

  • The tetrapeptide GPRP is a known affinity ligand for fibrinogen when immobilized.
  • Peptide synthesis directly onto chromatographic resins offers a novel approach for creating affinity media.

Purpose of the Study:

  • To demonstrate the effectiveness of synthesizing peptides directly onto amine-functionalized POROS resin for creating perfusive affinity media.
  • To evaluate the binding capacity and specificity of GPRP-POROS and GAQGHTVEK-POROS columns for fibrinogen and albumin, respectively.

Main Methods:

  • Synthesis of the GPRP peptide directly onto an amine-functionalized POROS resin.
  • Synthesis of a simplified peptide analogue GAQGHTVEK directly onto POROS resin.
  • Frontal analysis was used to determine the dynamic binding capacity of the columns.

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Main Results:

  • The GPRP-POROS column demonstrated specific binding of fibrinogen from plasma with a dynamic binding capacity of 10.2 mg/ml, and eluted bound fibrinogen showed weak clotting activity.
  • The GAQGHTVEK-POROS column specifically bound human serum albumin with a dynamic binding capacity of 19 mg/ml, allowing purification under non-denaturing conditions.
  • Both peptide columns showed specificity, not binding denatured fibrinogen and purifying albumin under non-denaturing conditions.

Conclusions:

  • Direct peptide synthesis onto POROS resin is an effective method for generating perfusive affinity media.
  • These novel affinity media exhibit high binding capacities and specificity for target proteins like fibrinogen and albumin.
  • This approach offers a promising strategy for efficient and non-denaturing protein purification.