Fig. 5: AC could directly bind to HBB with highest binding affinity. | Acta Pharmacologica Sinica

Fig. 5: AC could directly bind to HBB with highest binding affinity.

From: HBB contributes to individualized aconitine-induced cardiotoxicity in mice via interfering with ABHD5/AMPK/HDAC4 axis

Fig. 5

a The solvent-induced protein precipitation (SIP) combined with proteomics were utilized to identify the key targets for AC-associated cardiotoxicity. b CO-IP assay was applied to verify the combination of AC with HBB, ADH1, ABHD5, and AMPK. AC at 1 µM and 10 µM were used as concentration gradient to further confirm the bind of HBB with these proteins. c–f Docking data indicated the interactions of AC with HBB, ADH1, ABHD5, and AMPK, respectively and precise amino acids involved.

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