Fig. 6: Pb2+ can directly bind to HIF-1α inhibiting its degradation by Molecular docking and MD simulation. | Communications Biology

Fig. 6: Pb2+ can directly bind to HIF-1α inhibiting its degradation by Molecular docking and MD simulation.

From: Lead binds HIF-1α contributing to depression-like behaviour through modulating mitochondria-associated astrocyte ferroptosis

Fig. 6

A Molecular docking model illustrating the binding of Pb2+ to HIF-1α. Detailed interaction view (enlarged panel); B P138 of HIF-1α (marked in red) is conserved between different mammals; C Interaction energy between Pb2+ and HIF-1α; D The Rg of the HIF-1α protein and the Pb2 + -HIF-1α complex system; E. The RMSF of the HIF-1α protein and the Pb2 + -HIF-1α complex system; F The RMSF of the HIF-1α protein and the Pb2 + -HIF-1α complex system in different PRO residue; G The RMSD of the HIF-1α protein and the Pb2 + -HIF-1α complex system; H Conformational changes of the HIF-1α- Pb2+ complex in MD simulation; I Immunofluorescence assay was conducted to detect the Pb2+ and HIF-1α in astrocytes following Pb exposure; J UV-Vis absorption spectra, K Synchronous fluorescence spectra and (L) Circular dichroism spectrum of HIF-1α and Pb2+- HIF-1α systems (T = 298 K), C(HIF-1α) = 0.25 μM, C(Pb2+) (1 → 4): 0, 0.5, 1, 2 μM.

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