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