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Related Experiment Videos

Studies on selectin-carbohydrate interactions

G S Jacob1, J K Welply, P R Scudder

  • 1Department of Immunology, Searle Discovery Research, Monsanto Company, St. Louis, Missouri 63167, USA.

Advances in Experimental Medicine and Biology
|January 1, 1995
PubMed
Summary
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Multivalent sialyl Lewisx (sLex) conjugated to BSA significantly enhances binding affinity to E-selectin, offering a potent strategy for inhibiting neutrophil recruitment in inflammation.

Area of Science:

  • Biochemistry
  • Immunology
  • Glycoscience

Background:

  • Neutrophil recruitment to inflamed endothelium is crucial for immune response.
  • This process involves selectin-mediated rolling interactions between neutrophils and endothelial cells.
  • Selectins recognize specific carbohydrate structures, with multivalent binding enhancing interaction strength.

Purpose of the Study:

  • To investigate the potential of multivalent molecular antagonists to mimic and inhibit selectin-mediated cell-cell interactions.
  • To synthesize and test BSA-conjugated forms of sialyl Lewisx (sLex) for enhanced binding affinity to E-selectin.

Main Methods:

  • Synthesis of monovalent sLex and its BSA-conjugated forms.
  • Testing the inhibitory effects of these compounds on HL-60 cell binding to immobilized E-selectin.

Related Experiment Videos

  • Measurement of thermodynamic dissociation constants for monovalent sLex:E-selectin interactions.

    • Main Results:

    • BSA-conjugated sLex (sLex-BSA) demonstrated potent, dose-dependent inhibition of HL-60 cell binding to E-selectin.
    • sLex16-BSA exhibited a three-order of magnitude enhancement in inhibitory activity compared to free sLex, with an IC50 of 1 microM.
    • The thermodynamic dissociation constant for monovalent sLex:E-selectin interaction was determined to be 120 ± 31 microM.

    Conclusions:

    • Multivalent sLex-BSA exhibits significantly higher affinity for E-selectin than monovalent sLex.
    • This enhanced affinity suggests that multivalent glycan structures are effective in inhibiting selectin-mediated cell adhesion.
    • These findings support the development of multivalent antagonists for therapeutic intervention in inflammatory diseases.