Construction of a hyperbranched supramolecular polymer as a bifunctional antioxidative enzyme model

Abstract

A HBSP has been designed as a novel bifunctional enzyme model with SOD and GPx activity by host/guest-directed self-assembly of MnTPyP-M-Ad and 6-Te-diCD. The structure of the host/guest complex was elucidated by (1) H NMR spectra, and the HBSP was characterized by SEM, DLS and measurement of catalytic properties. In the bifunctional enzyme model, the Mn(III) porphyrins act as efficient SOD active sites and the tellurol moieties endow GPx activity. The SOD-like activity (IC(50) ) of this new supramolecular catalyst was found to be 1.05 × 10(-7) M, which corresponds to 2.82% of the activity of the native SOD enzyme. Besides this, the hyperbranched supramolecular polymer also shows a higher GPx activity (ν(0 ) = 21.7 × 10(-6) M · min(-1) ) than other supramolecular enzyme models.