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Title: Rational design of an organometallic glutathione transferase inhibitor

Abstract

A hybrid organic-inorganic (organometallic) inhibitor was designed to target glutathione transferases. The metal center is used to direct protein binding, while the organic moiety acts as the active-site inhibitor. The mechanism of inhibition was studied using a range of biophysical and biochemical methods.

Authors:
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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1006135
Resource Type:
Journal Article
Resource Relation:
Journal Name: Angew. Chem. Int. Ed.; Journal Volume: 48; Journal Issue: (21) ; 2009
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; BIOLOGY; CHEMISTRY; DESIGN; GLUTATHIONE; PROTEINS; TARGETS; TRANSFERASES

Citation Formats

Ang, W.H., Parker, L.J., De Luca, A., Juillerat-Jeanneret, L., Morton, C.J., LoBello, M., Parker, M.W., Dyson, P.J., and ISIC). Rational design of an organometallic glutathione transferase inhibitor. United States: N. p., 2010. Web.
Ang, W.H., Parker, L.J., De Luca, A., Juillerat-Jeanneret, L., Morton, C.J., LoBello, M., Parker, M.W., Dyson, P.J., & ISIC). Rational design of an organometallic glutathione transferase inhibitor. United States.
Ang, W.H., Parker, L.J., De Luca, A., Juillerat-Jeanneret, L., Morton, C.J., LoBello, M., Parker, M.W., Dyson, P.J., and ISIC). 2010. "Rational design of an organometallic glutathione transferase inhibitor". United States. doi:.
@article{osti_1006135,
title = {Rational design of an organometallic glutathione transferase inhibitor},
author = {Ang, W.H. and Parker, L.J. and De Luca, A. and Juillerat-Jeanneret, L. and Morton, C.J. and LoBello, M. and Parker, M.W. and Dyson, P.J. and ISIC)},
abstractNote = {A hybrid organic-inorganic (organometallic) inhibitor was designed to target glutathione transferases. The metal center is used to direct protein binding, while the organic moiety acts as the active-site inhibitor. The mechanism of inhibition was studied using a range of biophysical and biochemical methods.},
doi = {},
journal = {Angew. Chem. Int. Ed.},
number = (21) ; 2009,
volume = 48,
place = {United States},
year = 2010,
month = 8
}