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.

journal_name

Macromol Biosci

authors

Yu S,Zhang W,Zhu J,Yin Y,Jin H,Zhou L,Luo Q,Xu J,Liu J

doi

10.1002/mabi.201000478

subject

Has Abstract

pub_date

2011-06-14 00:00:00

pages

821-7

issue

6

eissn

1616-5187

issn

1616-5195

journal_volume

11

pub_type

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