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Related Experiment Videos

An E-selectin binding assay based on a polyacrylamide-type glycoconjugate

G Weitz-Schmidt1, D Stokmaier, G Scheel

  • 1Preclinical Research, Sandoz Pharma Ltd., Basel, CH-4002, Switzerland.

Analytical Biochemistry
|July 1, 1996
PubMed
Summary

We developed a sensitive assay using sialyl Lewis A polymers to detect E-selectin binding. This method aids in identifying and characterizing E-selectin antagonists for potential therapeutic applications.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Immunology

Background:

  • E-selectin is a cell adhesion molecule involved in inflammatory processes.
  • Sialyl Lewis X (sLex) and sialyl Lewis A (sLea) are carbohydrate ligands for E-selectin.

Purpose of the Study:

  • To establish a sensitive cell-free binding assay for characterizing E-selectin antagonists.
  • To utilize sialyl Lewis A polymers as ligands for E-selectin in the assay.

Main Methods:

  • Biotinylated sLea-polymer complexed with streptavidin-peroxidase.
  • Incubation with immobilized E-selectin mouse Ckappa fusion protein.
  • Detection of bound complex via peroxidase reaction, measuring Ca2+-dependent binding.

Main Results:

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  • sLea-polymer demonstrated higher affinity for E-selectin than sLex-polymer.
  • The assay showed specificity, with control glycoconjugates and anti-E-selectin antibodies blocking binding.
  • sLex partially inhibited sLea-polymer binding (IC50 550 microM).
  • Polymeric sLea inhibitors showed increased activity with higher sLea content (low micromolar IC50s).

Conclusions:

  • A sensitive, rapid, and simple cell-free assay for E-selectin ligand binding was established.
  • The assay is suitable for identifying and characterizing novel E-selectin antagonists.
  • sLea-polymers are effective ligands and multivalent inhibitors of E-selectin.