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7.
Scheme 1

Scheme 1. From: Design, Synthesis, and Biological Evaluation of Resveratrol Analogues as Aromatase and Quinone Reductase 2 Inhibitors for Chemoprevention of Cancer.

Reagents and conditions: (i) CH3PPh3Br, NaNH2, Et2O, rt; (ii) KOAc, Pd(OAc)2, Bu4NBr, DMF, 50–80 °C.

Bin Sun, et al. Bioorg Med Chem. ;18(14):5352-5366.
8.
Figure 3

Figure 3. From: Design, Synthesis, and Biological Evaluation of Resveratrol Analogues as Aromatase and Quinone Reductase 2 Inhibitors for Chemoprevention of Cancer.

Region of a 2D 1H-1H NOESY spectrum of 82. The red circle indicates the NOE signal of H8 and H17/21.

Bin Sun, et al. Bioorg Med Chem. ;18(14):5352-5366.
9.
Figure 5

Figure 5. From: Design, Synthesis, and Biological Evaluation of Resveratrol Analogues as Aromatase and Quinone Reductase 2 Inhibitors for Chemoprevention of Cancer.

Design of the novel resveratrol analogues based on the docking result of compound 32.

Bin Sun, et al. Bioorg Med Chem. ;18(14):5352-5366.
10.
Scheme 6

Scheme 6. From: Design, Synthesis, and Biological Evaluation of Resveratrol Analogues as Aromatase and Quinone Reductase 2 Inhibitors for Chemoprevention of Cancer.

Reagents and conditions: (i) NaBH4, THF; (ii) PBr3, DCM; (iii) PPh3, toluene, reflux; (iv) Imidazole, THF, rt; (v) H2, Pd/C, MeOH; (vi) K2CO3, 18-crown-6, DCM, reflux; (vii) SnCl2, EtOH, reflux.

Bin Sun, et al. Bioorg Med Chem. ;18(14):5352-5366.
11.
Figure 6

Figure 6. From: Design, Synthesis, and Biological Evaluation of Resveratrol Analogues as Aromatase and Quinone Reductase 2 Inhibitors for Chemoprevention of Cancer.

Potential interactions between compound 84 and Ile305, Asp309, Thr310, Trp224, Val370, Met374 and heme in human aromatase active site. The hydrogen bonds are labeled as yellow broken lines.

Bin Sun, et al. Bioorg Med Chem. ;18(14):5352-5366.
12.
Scheme 5

Scheme 5. From: Design, Synthesis, and Biological Evaluation of Resveratrol Analogues as Aromatase and Quinone Reductase 2 Inhibitors for Chemoprevention of Cancer.

Reagents and conditions: (i) TBDMSCl, DIPEA, DMF; (ii) CH3PPh3Br, NaNH2, Et2O; (iii) TBAF, THF; (iv) Ac2O, DMAP, DCM; (v) KOAc, Pd(OAc)2, Bu4NBr, DMF, 70 °C, 10 h; (vi) NaOMe, MeOH.

Bin Sun, et al. Bioorg Med Chem. ;18(14):5352-5366.
13.
Figure 4

Figure 4. From: Design, Synthesis, and Biological Evaluation of Resveratrol Analogues as Aromatase and Quinone Reductase 2 Inhibitors for Chemoprevention of Cancer.

(A) Ribbon diagram illustrating the hypothetical complex structure of human aromatase with compound 32 bound to the active site, and the hydrogen bonds are labeled as yellow broken lines. (B) Potential interactions between compound 32 and Ile305, Asp309, Thr310, Trp224, Val370, Met374 in human aromatase active site. The hydrogen bonds are labeled as yellow broken lines.

Bin Sun, et al. Bioorg Med Chem. ;18(14):5352-5366.
14.
Figure 7

Figure 7. From: Design, Synthesis, and Biological Evaluation of Resveratrol Analogues as Aromatase and Quinone Reductase 2 Inhibitors for Chemoprevention of Cancer.

High-resolution X-ray Structures of human QR2 in complex with resveratrol (A), compound 32 (B) and compound 44 (C). All panels are presented in walleyed stereoviews showing the FAD cofactor and the active site residues Asn161 and Thr71. Active site water molecules are shown as red spheres and hydrogen bonds are shown as dashed lines. 2Fo-Fc electron density maps are contoured to 1 σ. Carbon atoms and bonds are colored blue for resveratrol, green for compound 32 and cyan for compound 44. The X-ray structure of the QR2-resveratrol complex is from PDB code 1SG0.

Bin Sun, et al. Bioorg Med Chem. ;18(14):5352-5366.

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