Facile incorporation of urea pseudopeptides into protease substrate analogue inhibitors

AC Myers, JA Kowalski, MA Lipton

Index: Myers, Adam C.; Kowalski, Jennifer A.; Lipton, Mark A. Bioorganic and Medicinal Chemistry Letters, 2004 , vol. 14, # 20 p. 5219 - 5222

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Citation Number: 34

Abstract

A new procedure that employs a one-pot, oxidative Hofmann rearrangement to incorporate a urea linkage into peptide backbones is detailed herein. This methodology was used to replace the scissile peptide bonds of [Leu5] enkephalin and a hexapeptide HIV-1 protease substrate. The [Leu5] enkephalin analogue was found to inhibit cleavage of hippurylhistidylleucine (HHL) by porcine kidney angiotensin-converting enzyme (PK-ACE) ...