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Design of Artificial Selenoenzymes Based on Macromolecular Scaffolds
Author(s) -
Huang Xin,
Yin Yanzhen,
Liu Junqiu
Publication year - 2010
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201000134
Subject(s) - macromolecule , artificial enzyme , supramolecular chemistry , catalysis , chemistry , nanotechnology , peroxidase , combinatorial chemistry , biochemical engineering , biochemistry , enzyme , materials science , organic chemistry , engineering , molecule
The selenoenzyme glutathione peroxidase has received increased attention as one of the antioxidative enzymes exerting important biological roles in living bodies. Over the past decades, much effort has been invested to mimic its catalytic behavior for understanding enzymatic catalytic mechanisms and also for developing potential medicines. A great number of artificial GPxs, ranging from small molecular compounds to macromolecular ones, have been designed and prepared by combining the concept of recognition and catalysis using chemical, biological and supramolecular strategies. In this article, we specify the development of artificial GPxs based on macromolecules as scaffolds, and discuss the power of reduced models in studying the bio‐catalytic nature of selenoenzymes.