Selective inhibition of low affinity IgE receptor (CD23) processing : P1' bicyclomethyl substituents

Using a variety of alpha-hydroxy hydroxamic acid derivatives, the size and shape of the S1' pocket for the CD23 processing metalloprotease has been explored. It has been demonstrated that a P1' 2-naphthylmethyl group occupies most of the available space and gives excellent selectivity agai...

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters 1999-11, Vol.9 (21), p.3165-3170
Hauptverfasser:	BAILEY, S, BOLOGNESE, B, WARD, J. G, FALLER, A, LOUIS-FLAMBERG, P, MACPHERSON, D. T, MAYER, R. J, MARSHALL, L. A, MILNER, P. H, MISTRY, J, SMITH, D. G
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Bridged Bicyclo Compounds - chemical synthesis Bridged Bicyclo Compounds - pharmacology Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - pharmacology Hydroxamic Acids - chemical synthesis Hydroxamic Acids - pharmacology Immunomodulators Matrix Metalloproteinase Inhibitors Medical sciences Molecular Structure Pharmacology. Drug treatments Receptors, IgE - antagonists & inhibitors Receptors, IgE - metabolism Structure-Activity Relationship
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Zusammenfassung:	Using a variety of alpha-hydroxy hydroxamic acid derivatives, the size and shape of the S1' pocket for the CD23 processing metalloprotease has been explored. It has been demonstrated that a P1' 2-naphthylmethyl group occupies most of the available space and gives excellent selectivity against fibroblast collagenase (matrix metalloproteinase-1, MMP-1) and other MMPs.
ISSN:	0960-894X 1464-3405
DOI:	10.1016/S0960-894X(99)00552-1