earticle

영어

Accumulation of heavy metals is one of the major concerns for the environmental safety because of their toxicity and non-degradability. In particular, cadmium and several cadmium-containing compounds are known as carcinogens and can induce many types of cancer. Among promising strategies of cadmium removal, one emerging technology is the use of tunable, metal binding biopolymers based on elastin-like polypeptides (ELPs). An ELP consisting of the repeating
pentapeptide of specific amino acids, Val-Pro-Gly-Xaa-Gly (where the “guest residue” Xaa is any amino except Proline), undergoes a reversible phase transition at a specific temperature (transition temperature, Tt). For effective elimination of cadmium, synthetic phytochelatin (EC),
which is a metal-binding protein and has a repetitive motif (Glu-Cys)nGly, was fused with the ELP. We expected that a fusion protein constituting ELP and EC can detect and remove cadmium without any complex process. In this study, a fusion protein was expressed in E.coli and metal binding ability of EC to cadmium was examined quantitatively. In addition, transition temperature variation when the fusion protein binds cadmium was analyzed.