Abstract
The effect of dopamine (DA) on the nucleation and growth rate of hen egg white lysozyme (HEWL) crystals was studied using polarizing microscopy, powder X-ray diffraction, fluorescence spectroscopy, circular dichroism, and dynamic light scattering, in combination with molecular dynamic simulations. DA increased the solubility of HEWL and promoted the nucleation of HEWL crystals. Crystallization experiments also showed that the shape of HEWL crystals changed from a block to a rod with DA addition, which was attributed to the variation in the growth rates of their neighboring planes. The growth of (101) plane was slightly inhibited and decreased from 3.9 to 3.1 nm/s while the growth rate of (110) decreased significantly from 4.1 to 1.8 nm/s with an increase of DA content. Molecular dynamic simulations indicated that hydrogen bonding and hydrophobic interactions between DA and HEWL were mainly concentrated in the pocket region of HEWL, which enhanced the hydrophilicity and steric hindrance of the area, modulated the assembly behavior of HEWL, and resulted in the anisotropic growth of HEWL crystals. These results suggest that small organic molecules in vivo are an important factor in modulating protein crystal morphology by adjusting the conformational structure of protein molecules.
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