nor-beta-lapachone and dunnione

nor-beta-lapachone has been researched along with dunnione* in 1 studies

Other Studies

1 other study(ies) available for nor-beta-lapachone and dunnione

Article	Year
Synthesis and evaluation of (±)-dunnione and its ortho-quinone analogues as substrates for NAD(P)H:quinone oxidoreductase 1 (NQO1). Bioorganic & medicinal chemistry letters, 2015, Mar-15, Volume: 25, Issue:6 Natural product (±)-dunnione (2) and its ortho-quinone analogues (3-8) were synthesized and found to be substrates for NQO1. The structure-activity relationship study revealed that the biological activity was favored by the presence of methyl group at the C ring and methoxy group at the A ring. The docking studies supported the rationalization of the metabolic studies. Deeper location in the active site of NQO1, interactions with hydrophobic pocket and C-H…π interactions with the adjacent Phe178 residue contributed to the better catalytic efficiency and specificity to NQO1. Cytotoxicity studies and determination of superoxide (O2(-)) production in the presence and absence of the NOQ1 inhibitor dicoumarol confirmed that the ortho-quinones exerted their antitumor activity through NQO1-mediated ROS production by redox cycling. Topics: Binding Sites; Catalytic Domain; Cell Line, Tumor; Cell Survival; Enzyme Inhibitors; Humans; Kinetics; Molecular Docking Simulation; NAD(P)H Dehydrogenase (Quinone); Naphthoquinones; Quinones; Reactive Oxygen Species; Stereoisomerism; Structure-Activity Relationship; Substrate Specificity; Superoxides	2015

Article

Year

Synthesis and evaluation of (±)-dunnione and its ortho-quinone analogues as substrates for NAD(P)H:quinone oxidoreductase 1 (NQO1).

Bioorganic & medicinal chemistry letters, 2015, Mar-15, Volume: 25, Issue:6

Natural product (±)-dunnione (2) and its ortho-quinone analogues (3-8) were synthesized and found to be substrates for NQO1. The structure-activity relationship study revealed that the biological activity was favored by the presence of methyl group at the C ring and methoxy group at the A ring. The docking studies supported the rationalization of the metabolic studies. Deeper location in the active site of NQO1, interactions with hydrophobic pocket and C-H…π interactions with the adjacent Phe178 residue contributed to the better catalytic efficiency and specificity to NQO1. Cytotoxicity studies and determination of superoxide (O2(-)) production in the presence and absence of the NOQ1 inhibitor dicoumarol confirmed that the ortho-quinones exerted their antitumor activity through NQO1-mediated ROS production by redox cycling.

Topics: Binding Sites; Catalytic Domain; Cell Line, Tumor; Cell Survival; Enzyme Inhibitors; Humans; Kinetics; Molecular Docking Simulation; NAD(P)H Dehydrogenase (Quinone); Naphthoquinones; Quinones; Reactive Oxygen Species; Stereoisomerism; Structure-Activity Relationship; Substrate Specificity; Superoxides

2015