Amino Acids and Peptides. XLIV. Synthesis of Stereoisomeric Pentapeptides of Thiol Proteinase Inhibitor

• Published in: Chemical & pharmaceutical bulletin Vol. 44; no. 8; pp. 1599 - 1602
• Main Authors: IGUCHI, Shin, HIRANO, Kenichi, OKAMOTO, Hiroshi, OKAMOTO, Yoshiko, OKADA, Yoshio
• Format: Journal Article
• Language: English
• Published: Tokyo The Pharmaceutical Society of Japan 1996; Maruzen; Japan Science and Technology Agency
• Subjects: Amino Acid Sequence; Amino Acids - analysis; Analytical, structural and metabolic biochemistry; Biological and medical sciences; circular dichroism spectra; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; Indicators and Reagents; Molecular Sequence Data; Oligopeptides - analysis; Oligopeptides - chemical synthesis; Papain - antagonists & inhibitors; Protease Inhibitors - analysis; Protease Inhibitors - chemical synthesis; Spectrophotometry, Ultraviolet; stereoisomeric pentapeptide; Stereoisomerism; structure-activity relationship; thiol proteinase inhibitor; TPI common sequence; Circular dichroism spectrum; Peptides; Enzyme; Cysteine endopeptidases; Enzyme inhibitor; Papain; In vitro; Structure activity relation; Hydrolases; Carboxamide; Peptide synthesis; Chemical synthesis; Proteinases; Pentapeptide
• ISSN: 0009-2363; 1347-5223
• DOI: 10.1248/cpb.44.1599

Stereoisomers of thiol proteinase inhibitor (TPI) were synthesized by a conventional solution method. Among them, iNoc-D-Gln-Val-Ala-Ala-pNA weakly inhibited the aminolytic activity of papain, although iNoc-Gln-Val-Val-Ala-Ala-pNA inhibited papain activity fairly potently. However, the other five D-amino acid-containing peptides did not show any inhibitor effects on papain. The circular dichroism (CD) spectra of the enzyme-peptides mixtures were measured in order to study the relationship between the peptide anilides-papain interaction and the inhibitory activity.