PEPTIDIC P-NITROANILIDE SUBSTRATES OF INTERLEUKIN-1-BETA-CONVERTING ENZYME

• Published in: International journal of peptide and protein research Vol. 43; no. 1; pp. 87 - 96
• Main Author: REITER, LA
• Format: Journal Article
• Language: English
• Published: COPENHAGEN Wiley 01.01.1994
• Subjects: Amino Acid Sequence; Amino Acids; Anilides - chemical synthesis; Anilides - metabolism; Aniline Compounds - chemistry; Aspartic Acid - chemistry; Biochemistry & Molecular Biology; Caspase 1; Colorimetry; Fluorenes; Life Sciences & Biomedicine; Metalloendopeptidases - antagonists & inhibitors; Metalloendopeptidases - metabolism; Molecular Sequence Data; Oligopeptides - chemical synthesis; Oligopeptides - metabolism; Science & Technology; Substrate Specificity; INTERLEUKIN-1-BETA-CONVERTING ENZYME; ICE; P-NITROANILIDE; SODIUM PERBORATE; ACID PARA-NITROANILIDES; PROTEASE
• ISSN: 0367-8377
• DOI: 10.1111/j.1399-3011.1994.tb00379.x

Peptidic p-nitroanilides are useful colorimetric substrates for enzymes. With the aim of developing a convenient, quantitative assay for inhibitors of interleukin-1beta-converting enzyme (ICE), we have explored three approaches to the synthesis of peptidic p-nitroanilides relevant to this enzyme. The first approach involved a late stage oxidation of a p-aminoanilide such as CbzValAlaAsp(beta-tert-butyl)-p-(t-Boc-amino)anilide. The second and third approaches used the preformed amino acid p-nitroanilides HAsp-p-nitroanilide hydrochloride and HAsp(beta-tert-butyl)-p-nitroanilide which were coupled iteratively with preactivated amino acid derivatives or with an appropriate peptide, respectively. While each approach had it merits and limitations, all three produced p-nitroanilides that were substrates for ICE. (C) Munksgaard 1994.