Screening and chromatographic assessing of a novel IgG biomimetic ligand

Biomed Chromatogr. 2006 Oct;20(10):1109-15. doi: 10.1002/bmc.654.

Abstract

A novel biomimetic ligand, N-benzyloxycarbonyl-l-tyrosine (N-cbz-l-Tyr), was screened by a combination method of molecular docking and immobilized receptor technique. Then, N-cbz-l-Tyr was immobilized on Sepharose CL-4B to prepare a specific affinity adsorbent for immunoglobulin G (IgG). Scatchard analysis of the binding isotherm for IgG on the adsorbent gave an association constant (K(a)) of 4.91 x 10(6) m(-1) and a theoretical maximum adsorption capacity of 17.3 mg IgG/mL gel. IgG with a purity of 98% was separated from human plasma by this new affinity adsorbent.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomimetic Materials / chemistry*
  • Biomimetics / methods
  • Chromatography, Affinity / methods*
  • Humans
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / isolation & purification*
  • Ligands
  • Models, Molecular
  • Molecular Mimicry
  • Molecular Structure
  • Reproducibility of Results
  • Sepharose / analogs & derivatives
  • Sepharose / chemistry
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
  • Tyrosine / analogs & derivatives*
  • Tyrosine / chemistry

Substances

  • Immunoglobulin G
  • Ligands
  • N-benzyloxycarbonyl-l-tyrosine
  • Tyrosine
  • Sepharose CL 4B
  • Sepharose