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Bioorg Med Chem Lett. 2009 Jul 1;19(13):3525-30. doi: 10.1016/j.bmcl.2009.04.143. Epub 2009 May 5.

Compelling P1 substituent affect on metalloprotease binding profile enables the design of a novel cyclohexyl core scaffold with excellent MMP selectivity and HER-2 sheddase inhibition.

Author information

1
Incyte Corporation, Department of Medicinal Chemistry, Wilmington, DE 19880, USA. dburns@incyte.com

Abstract

A serendipitous discovery that the metalloprotease binding profile of a novel class of 2-carboxamide-3-hydroxamic acid piperidines could be significantly attenuated by the modification of the unexplored P1 substituent enabled the design and synthesis of a novel 2-carboxamide-1-hydroxamic acid cyclohexyl scaffold core that exhibited excellent HER-2 potency and unprecedented MMP-selectivity that we believe would not have been possible via conventional P1' perturbations.

PMID:
19457660
DOI:
10.1016/j.bmcl.2009.04.143
[Indexed for MEDLINE]

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