Inhibitory assay for degradation of collagen IV by cathepsin B with a surface plasmon resonance sensor.

J Pharm Biomed Anal

Department of Chemistry, College of Humanities and Sciences, Nihon University, Sakurajousui, Setagaya, Tokyo 156-8550, Japan. Electronic address:

Published: October 2017

AI Article Synopsis

  • The study presents a method using a surface plasmon resonance (SPR) biosensor to assess how effectively different inhibitors prevent the breakdown of collagen IV by the enzyme cathepsin B.
  • SPR signal changes showed that higher concentrations of inhibitors led to decreased enzyme activity, with a specific order of effectiveness for each inhibitor.
  • The findings indicate that CA074 and Z-Phe-Phe-FMK primarily inhibit exopeptidase activity, while leupeptin is a stronger inhibitor of endopeptidase activity in cathepsin B.

Article Abstract

We describe a simple method for evaluating the inhibition of collagen IV degradation by cathepsin B with a surface plasmon resonance (SPR) biosensor. The change in the SPR signal decreased with an increase in the concentration of cathepsin B inhibitors. The order of the inhibitory constant (Ki) obtained by the SPR method was CA074Me≈Z-Phe-Phe-FMK < leupeptin. This order was different from that obtained by benzyloxycarbonyl-Phe-Phe-Fluoromethylketone (Z-Phe-Phe-FMK) as a peptide substrate. The comparison of Ki suggested that CA074 and Z-Phe-Phe-FMK inhibited exopeptidase activity, and leupeptin inhibited the endopeptidase activity of cathepsin B more strongly.

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http://dx.doi.org/10.1016/j.jpba.2017.06.026DOI Listing

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