Figure 2.
Figure 2. Phthalides stabilize oxyHbF in the low-oxygen-affinity state. RR spectroscopy of oxyHbF treated with varying amounts of 2,3-BPG (A), z-butylidenephthalide (B), and z-ligustilide (C) and deoxyHbF treated with varying amounts of 2,3-BPG (D), z-butylidenephthalide (E), and z-ligustilide (F). Color code for panels A-F: pure HbF (gray), HbF treated with the specified effector of 1 mM (red), 4 mM (orange), 8 mM (green), and 12 mM (violet). (G) Percentages of the high-affinity state for oxyHbF treated with z-butylidenephthalide (purple curve), z-ligustilide (orange curve), and 2,3-BPG (gray curve) with increasing degrees of treatment. (H) Active sites of HbF upon treatment with z-butylidenephthalide, with the intermolecular interactions denoted as yellow dashed lines. (I) Active sites of HbF upon treatment with z-ligustilide, with the intermolecular interactions denoted as yellow dashed lines.

Phthalides stabilize oxyHbF in the low-oxygen-affinity state. RR spectroscopy of oxyHbF treated with varying amounts of 2,3-BPG (A), z-butylidenephthalide (B), and z-ligustilide (C) and deoxyHbF treated with varying amounts of 2,3-BPG (D), z-butylidenephthalide (E), and z-ligustilide (F). Color code for panels A-F: pure HbF (gray), HbF treated with the specified effector of 1 mM (red), 4 mM (orange), 8 mM (green), and 12 mM (violet). (G) Percentages of the high-affinity state for oxyHbF treated with z-butylidenephthalide (purple curve), z-ligustilide (orange curve), and 2,3-BPG (gray curve) with increasing degrees of treatment. (H) Active sites of HbF upon treatment with z-butylidenephthalide, with the intermolecular interactions denoted as yellow dashed lines. (I) Active sites of HbF upon treatment with z-ligustilide, with the intermolecular interactions denoted as yellow dashed lines.

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