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  • 标题:Isolation of Novel Peptides, Cabin-1, -2, -3, and -4, That Inhibit Cathepsin B from a Thermolysin Digest of Human Plasma
  • 本地全文:下载
  • 作者:Kazuya Nakagomi ; Akiyoshi Fujimura ; Hiromi Maeda
  • 期刊名称:Biological and Pharmaceutical Bulletin
  • 印刷版ISSN:0918-6158
  • 电子版ISSN:1347-5215
  • 出版年度:2002
  • 卷号:25
  • 期号:5
  • 页码:564-568
  • DOI:10.1248/bpb.25.564
  • 出版社:The Pharmaceutical Society of Japan
  • 摘要:Four novel peptides that inhibit cathepsin B, designated as Cabin-1, -2, -3, and -4, were isolated from a thermolysin digest of human plasma. After gel filtration and cation-exchange chromatography, the peptide mixture was purified by reverse-phase HPLC to isolate Cabin-1, -2, -3, and 4, with the amino acid sequences LGPVTQE, VLQSSGLYS, VVSVLT, and LVYDAY, respectively. These peptides correspond to f(64—70) of human apolipoprotein A-I for Cabin-1, f(56—64) and f(185—190) of the human immunoglobulin G γ chain for Cabin-2 and -3, and f(66—71) of human transferrin for Cabin-4. Synthetic Cabin-1, -2, -3, and -4 showed dose-dependent inhibition of cathepsin B. Their IC50 values were 450, 500, 20, and 5.0 μmol/l, respectively. Lineweaver–Burk plots suggested that Cabin-3 is a noncompetitive inhibitor, while Cabin-4 is a competitive inhibitor. Among the N- and C-terminal deletion peptides of Cabin-2 and -4, Cabin-2(1—8), VLQSSGLY, was found to have the most potent inhibitory activity, with an IC50 of 3.8 μmol/l.
  • 关键词:Cabin-1, -2, -3, and -4;cathepsin B inhibitory peptide;thermolysin;enzymatic hydrolysate;human plasma
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