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• W2021002429 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) with a 0.88 mM IC50 value, comparable to the Michaelis constant of [Leu5]enkephalin with the same enzyme. The HIV-1 protease substrate analogue was shown to inhibit HIV-1 protease with an IC50=34 microM." @default.
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• W2021002429 date "2004-10-01" @default.
• W2021002429 modified "2023-09-27" @default.
• W2021002429 title "Facile incorporation of urea pseudopeptides into protease substrate analogue inhibitors" @default.
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• W2021002429 doi "https://doi.org/10.1016/j.bmcl.2004.07.092" @default.
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