Elucidation of crucial structures for a catechol-based inhibitor of plasma hyaluronan-binding protein (factor VII activating protease) autoactivation.

@article{Yamamoto2011ElucidationOC,
  title={Elucidation of crucial structures for a catechol-based inhibitor of plasma hyaluronan-binding protein (factor VII activating protease) autoactivation.},
  author={Eisaku Yamamoto and Yoshikazu Kitano and Keiji Hasumi},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2011},
  volume={75 10},
  pages={
          2070-2
        }
}
Plasma hyaluronan-binding protein (PHBP) is a serine protease the activation of which is implicated in inflammation. Previous investigations have suggested the presence of catechol-binding sites in its proenzyme form, pro-PHBP. Here we found that compounds with plural catechol groups conjugated with strong electron-withdrawing groups, such as tyrphostin AG 537 (IC(50)=18 nM), were potent inhibitors of pro-PHBP activation. 

References

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O O Conjugated system e− e− O O EWG(s) Fig. 3. Schematic Model of Crucial Structures for a Catechol-Based Inhibitor of Pro-PHBP Autoactivation

E. YAMAMOTO
  • Biosci. Biotechnol. Biochem.,
  • 2010