Table 5 Potential molecular interactions and binding affinities of AFM1 with tubulin proteins.

From: Toxicity mechanisms of aflatoxin M1 assisted with molecular docking and the toxicity-limiting role of trans-resveratrol

Macromolecule

Free energy of binding (kcal/mol

Inhibition constant (Ki)

Hydrogen bond interactions

Hydrophobic interactions

Tubulin alpha-1B chain

− 7.94

1.52 µM

GLN11 (×2), ALA12,ASN101, SER140, THR179, PHE141

ALA180 (×2), ILE171, ALA12,

Tubulin beta chain

− 7.08

6.44 µM

THR274, LEU228

LEU215, HIS227 (×3), ALA231, PRO272, LEU361, LEU228, PHE270

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