Structure-activity relationship studies of nordihydroguaiaretic acid inhibitors toward soybean, 12-human, and 15-human lipoxygenase

J Med Chem. 2002 Jun 6;45(12):2659-61. doi: 10.1021/jm0201262.

Abstract

Lipoxygenase (LO) is a biological target for many diseases such as asthma, atherosclerosis, and cancer. Our labs have synthesized and investigated nordihydroguaiaretic acid (NDGA) derivatives and have established that the reductive inhibition of soybean and 15-human LO can be affected by the strength of the electron-withdrawing substituents on the phenyl rings of NDGA. In addition, we have determined that hydrophobic NDGA derivatives activate 15-HLO, suggesting a hydrophobic allosteric site.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Allosteric Site
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Glycine max / enzymology
  • Humans
  • Lipoxygenase / metabolism*
  • Lipoxygenase Inhibitors*
  • Masoprocol / analogs & derivatives*
  • Masoprocol / chemical synthesis*
  • Masoprocol / chemistry
  • Masoprocol / pharmacology
  • Structure-Activity Relationship

Substances

  • Enzyme Inhibitors
  • Lipoxygenase Inhibitors
  • Masoprocol
  • lipoxygenase L-1
  • Lipoxygenase