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Structure–Activity Correlation between Natural Glutathione Peroxidase (GPx) and Mimics: A Biomimetic Concept for the Design and Synthesis of More Efficient GPx Mimics
Author(s) -
Mugesh Govindasamy,
du Mont WolfWalther
Publication year - 2001
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/1521-3765(20010401)7:7<1365::aid-chem1365>3.0.co;2-y
Subject(s) - glutathione peroxidase , peroxidase , chemistry , glutathione , substrate (aquarium) , enzyme , stereochemistry , biochemistry , combinatorial chemistry , biology , ecology
Among the organoselenium compounds that mimic the action of the natural enzyme glutathione peroxidase (GPx), there are certain basic differences in the activity, substrate specificity and mechanism. These differences arise mainly from the nature of the substituents near the reaction center, and stability and reactivity of the intermediates. As an attempt to draw some general concepts for the development of new mimics, a structure–activity correlation between natural GPx and some existing mimics is described.