Abstract
From the observation that the broad spectrum matrix metalloproteinase inhibitor batimistat was capable of inhibiting the release of the low affinity IgE receptor, CD23, from the cell membrane, it has been possible to identify N-hydroxamic acid derivatives that selectively inhibit sCD23 release. Further modifications have led to a series of selective inhibitors that lack any peptide bonds utilising either a secondary or, as here, a tertiary sulfonamide linkage to replace the peptide linkage.