Exploiting the interactions between poly-histidine fusion tags and immobilized metal ions

Wen-Hui K. Kuo (1) , Howard A. Chase (1)

1 Department of Chemical Engineering and Biotechnology

Immobilized metal affinity chromatography (IMAC) of proteins containing poly-histidine fusion tags is an efficient research tool for purifying recombinant proteins from crude cellular feedstocks at laboratory scale. Nevertheless, to achieve successful purification of large amounts of the target protein for critical therapeutic applications that demand the precise removal of fusion tags, it is important to also take into consideration issues such as protein quality, efficiency, cost effectiveness, and optimal affinity tag choice and design. Despite the many considerations described in this article, it is expected that enhanced selectivity, the primary consideration in the field of protein separation, will continue to see the use of IMAC in solving new purification challenges. In addition, the platform nature of this technology makes it an ideal choice in purifying proteins with unknown properties. Finally, the unique interaction between immobilized metal ions and poly-histidine fusion tag has enabled new developments in the areas of biosensor, immunoassay, and other analytical technologies.

Mots clés: Electrochemical immuno-sensor; Fusion tags; Immobilized metal affinity; Poly-histidine fusion tag cleavage; Proteins

Domaines: Biotechnologie; Biotechnologies

Wen-Hui K. Kuo, Howard A. Chase. Exploiting the interactions between poly-histidine fusion tags and immobilized metal ions. Biotechnology Letters, 2011, pp.1075-1084. ⟨10.1007/s10529-011-0554-3⟩. ⟨hal-00669198⟩