Structure-activity relationship studies of nordihydroguaiaretic acid inhibitors toward soybean, 12-human, and 15-human lipoxygenase.
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.
Whitman
Stephanie
S
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA.
Gezginci
Mikail
M
Timmermann
Barbara N
BN
Holman
Theodore R
TR
D000495:Allosteric Site; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D008084:Lipoxygenase / Q000378:metabolism*; D016859:Lipoxygenase Inhibitors; D009637:Masoprocol / Q000031:analogs & derivatives* / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D013025:Glycine max / Q000201:enzymology; D013329:Structure-Activity Relationship
D004791:Enzyme Inhibitors; D016859:Lipoxygenase Inhibitors; D009637:Masoprocol; C101084:lipoxygenase L-1; D008084:Lipoxygenase