Abstract
Petal-like ferric oxide/cysteine (FeOOH/Cys) architectures were prepared through a solvothermal route, which possessed high thiol group density. These thiol groups as binding sites can chelate Ni2+ ions, which can be further used to enrich and separate his-tagged proteins directly from the mixture of lysed cells without sample pretreatment. These results show that the FeOOH/Cys architectures with immobilized Ni2+ ions present negligible nonspecific protein adsorption and high protein adsorption capacity, with the saturation capacity being 88mg/g, which are especially suitable for purification of his-tagged proteins.
Published Version
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