Synthesis of petal-like ferric oxide/cysteine architectures and their application in affinity separation of proteins

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 Ni 2   + 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 Ni 2   + ions present negligible nonspecific protein adsorption and high protein adsorption capacity, with the saturation capacity being 88   mg/g, which are especially suitable for purification of his-tagged proteins.