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

Abstract

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.

• Authors: Eisaku Yamamoto, Yoshikazu Kitano, Keiji Hasumi
• Journal: Bioscience, biotechnology, and biochemistry (Biosci Biotechnol Biochem) Vol. 75 Issue 10 Pg. 2070-2 ( 2011) ISSN: 1347-6947 [Electronic] England
• PMID: 21979097 (Publication Type: Journal Article)

Chemical References

• Catechols
• Protease Inhibitors
• HABP2 protein, human
• Serine Endopeptidases
• catechol

Topics

• Catechols (chemistry, pharmacology)
• Enzyme Activation (drug effects)
• Humans
• Protease Inhibitors (chemistry, pharmacology)
• Serine Endopeptidases (metabolism)
• Structure-Activity Relationship