Literature DB >> 11330888

Structure-activity correlation between natural glutathione peroxidase (GPx) and mimics: a biomimetic concept for the design and synthesis of more efficient GPx mimics.

G Mugesh1, W W du Mont.   

Abstract

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.

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Year:  2001        PMID: 11330888     DOI: 10.1002/1521-3765(20010401)7:7<1365::aid-chem1365>3.0.co;2-y

Source DB:  PubMed          Journal:  Chemistry        ISSN: 0947-6539            Impact factor:   5.236


  3 in total

1.  Activation energies of selenoxide elimination from Se-substituted selenocysteine.

Authors:  Craig A Bayse; Benjamin D Allison
Journal:  J Mol Model       Date:  2006-05-25       Impact factor: 1.810

2.  Synthesis of Nanovesicular Glutathione Peroxidase Mimics with a Selenenylsulfide-Bearing Lipid.

Authors:  Mamoru Haratake; Yuri Tachibana; Yui Emaya; Sakura Yoshida; Takeshi Fuchigami; Morio Nakayama
Journal:  ACS Omega       Date:  2016-07-06

3.  Association mechanism of S-dinitrophenyl glutathione with two glutathione peroxidase mimics: 2, 2 cent-ditelluro- and 2, 2 cent-diseleno-bridged b-cyclodextrins.

Authors:  Ya-Qiong Hao; Xing-Chen Liu; Jun-Qiu Liu; Yu-Qing Wu
Journal:  Molecules       Date:  2009-02-25       Impact factor: 4.411

  3 in total

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