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The hydrophobic forces in the functional dynamics of membrane protein FABP4 are known to be modulated by the electrostatic interaction with the polyvalent (cationic) surfactants. However, it remains unclear how this affects the intrinsic dynamics of the hydrophobic protein, the general character of the electrostatic interaction, and the magnitude of the critical micellar concentration for the solvated protein. In this work, we demonstrate that the single domain protein FABP4 experiences dynamic changes in its ensemble behavior in the presence of the new type of polyvalent ionic surfactants, i.e., PEI-coated silica nanoparticles with a wide range of surface charges. Our dynamic studies indicate that the electrostatic coupling between the protein and the surfactant is modulated by the charge of the PEI coating. With negatively charged PEI-coated silica nanoparticles, the hydrophobic protein loses its dynamism. 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