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The synthesis and evaluation of peptidyl aspartyl aldehydes as inhibitors of ice.

โœ Scribed by Michael D. Mullican; David J. Lauffer; Roger J. Gillespie; Saroop S. Matharu; David Kay; Geoffrey M. Porritt; Phillip L. Evans; Julian M.C. Golec; Mark A. Murcko; Yu-Ping Luong; Scott A. Raybuck; David J. Livingston


Book ID
103982815
Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
306 KB
Volume
4
Category
Article
ISSN
0960-894X

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โœฆ Synopsis


The tetrapeptide aldehyde AC-Tyr-Val-Ala-AspH (1, L-709,049) has been reported to be a potent reversible inhibitor of Interleukln-1 B Converting E e (ICE). We have prepared a series of analogs of 1, in order to explore the active site of ICE. The e ects of truncation, methylation of the amide nitrogens and "x" modification of the aldehyde group of 1 are presented.


๐Ÿ“œ SIMILAR VOLUMES


Enzymatic synthesis of peptidyl amino al
โœ Joanna V. Potetinova; Tatiana L. Voyushina; Valentin M. Stepanov ๐Ÿ“‚ Article ๐Ÿ“… 1997 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 256 KB

An enzymatic synthesis of peptidyl amino alcohols is described. The reactions were performed in organic solvents using as a catalyst subtilisin distributed on the surface of macroporous silica. Subsequent mild oxidation of peptidyl amino alcohols results in peptide aldehydes -the potent specific inh