Synthesis and evaluation of diacylhydrazines as inhibitors of the interleukin-1β converting enzyme (ICE)

Todd L. Graybill; Roland E. Dolle; Carla T. Helaszek; Mark A. Ator; Joost Strasters

doi:10.1016/0960-894X(95)00194-X

Synthesis and evaluation of diacylhydrazines as inhibitors of the interleukin-1β converting enzyme (ICE)

Todd L. Graybill, Roland E. Dolle, Carla T. Helaszek, Mark A. Ator, Joost Strasters

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Abstract

Diacylhydrazines ([azaAsp¹] derivatives) were prepared and shown to inactivate ICE in a time-dependent manner. Inactivation rates for most of these diacylhydrazines were 10-fold slower than their α-substituted methylketone congeners. Rates for 6 and 7 (ca. 18,000 M^-1s^-1) compared favorably to those reported for Ac-Tyr-Val-Ala-Asp-CH-N₂ and azapeptide inhibitors for other cysteine proteases.

Original language	English
Pages (from-to)	1197-1202
Number of pages	6
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	5
Issue number	11
DOIs	https://doi.org/10.1016/0960-894X(95)00194-X
State	Published - Jun 8 1995

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title = "Synthesis and evaluation of diacylhydrazines as inhibitors of the interleukin-1β converting enzyme (ICE)",

abstract = "Diacylhydrazines ([azaAsp1] derivatives) were prepared and shown to inactivate ICE in a time-dependent manner. Inactivation rates for most of these diacylhydrazines were 10-fold slower than their α-substituted methylketone congeners. Rates for 6 and 7 (ca. 18,000 M-1s-1) compared favorably to those reported for Ac-Tyr-Val-Ala-Asp-CH-N2 and azapeptide inhibitors for other cysteine proteases.",

author = "Graybill, {Todd L.} and Dolle, {Roland E.} and Helaszek, {Carla T.} and Ator, {Mark A.} and Joost Strasters",

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T1 - Synthesis and evaluation of diacylhydrazines as inhibitors of the interleukin-1β converting enzyme (ICE)

AU - Graybill, Todd L.

AU - Dolle, Roland E.

AU - Helaszek, Carla T.

AU - Ator, Mark A.

AU - Strasters, Joost

PY - 1995/6/8

Y1 - 1995/6/8

N2 - Diacylhydrazines ([azaAsp1] derivatives) were prepared and shown to inactivate ICE in a time-dependent manner. Inactivation rates for most of these diacylhydrazines were 10-fold slower than their α-substituted methylketone congeners. Rates for 6 and 7 (ca. 18,000 M-1s-1) compared favorably to those reported for Ac-Tyr-Val-Ala-Asp-CH-N2 and azapeptide inhibitors for other cysteine proteases.

AB - Diacylhydrazines ([azaAsp1] derivatives) were prepared and shown to inactivate ICE in a time-dependent manner. Inactivation rates for most of these diacylhydrazines were 10-fold slower than their α-substituted methylketone congeners. Rates for 6 and 7 (ca. 18,000 M-1s-1) compared favorably to those reported for Ac-Tyr-Val-Ala-Asp-CH-N2 and azapeptide inhibitors for other cysteine proteases.

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U2 - 10.1016/0960-894X(95)00194-X

DO - 10.1016/0960-894X(95)00194-X

M3 - Article

AN - SCOPUS:0029002823

SN - 0960-894X

VL - 5

SP - 1197

EP - 1202

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 11

ER -

Synthesis and evaluation of diacylhydrazines as inhibitors of the interleukin-1β converting enzyme (ICE)

Abstract

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