J. Choay is the first author of a 1983 study testing which defined fragments of heparin support binding to antithrombin. The team synthesized related four- and five-sugar structures, checked their chemical structures by nuclear magnetic resonance, and measured binding and enhancement of factor Xa inhibition.[ref]
Structure-activity relationship in heparin: a synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity by J. Choay and others. Abstract; Biochemical and Biophysical Research Communications 116, 492–499, 1983
The tested five-sugar fragment formed an equimolar complex with antithrombin and enhanced its inhibitory activity; the four-sugar fragment did not show the same behavior. Comparing chemically defined fragments helped separate a particular residue arrangement from the heterogeneous mixture of chains in a heparin preparation. Structure confirmation and activity measurement answered different questions, and both were needed for the argument.[ref]
Structure-activity relationship in heparin: a synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity by J. Choay and others. Abstract: synthetic tetrasaccharide/pentasaccharide comparison, binding and anti-factor Xa activity
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