Table 3 Potential molecular interactions and binding affinities of AFM1 with histone 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

Histone H3.1

− 5.30

131.29 µM

THR59 (×2)

VAL62 (×4), LEU63, LEU97

Histone H4

− 5.43

105.48 µM

PHE70, VAL66

ILE69, ILE73 (×4), ALA110, ILE94, VAL98, PHE70

Histone H2A

− 6.92

8.44 µM

ARG72 (×2), GLN76

ARG72, ALA75, LEU82, ARG83, PHE84

Histone H2B type 1-A

− 5.05

198.56 µM

LYS59 (×2)

ILE26, LEU62 (×3), LYS59 (×2), ILE66, ILE29, LEU58

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