A nonpeptidyl mimic of superoxide dismutase with therapeutic activity in rats

Daniela Salvemini; Zhi Qiang Wang; Jay L. Zweier; Alexandre Samouilov; Heather Macarthur; Thomas P. Misko; Mark G. Currie; Salvatore Cuzzocrea; James A. Sikorski; Dennis P. Riley

doi:10.1126/science.286.5438.304

A nonpeptidyl mimic of superoxide dismutase with therapeutic activity in rats

Daniela Salvemini, Zhi Qiang Wang, Jay L. Zweier, Alexandre Samouilov, Heather Macarthur, Thomas P. Misko, Mark G. Currie, Salvatore Cuzzocrea, James A. Sikorski, Dennis P. Riley

School of Medicine

Research output: Contribution to journal › Article › peer-review

457 Scopus citations

Abstract

Many human diseases are associated with the overproduction of oxygen free radicals that inflict cell damage. A manganese(II) complex with a bis(cyclohexylpyridine)-substituted macrocyclic ligand (M40403) was designed to be a functional mimic of the superoxide dismutase (SOD) enzymes that normally remove these radicals. M40403 had high catalytic SOD activity and was chemically and biologically stable in vivo. Injection of M40403 into rat models of inflammation and ischemia-reperfusion injury protected the animals against tissue damage. Such mimics may result in better clinical therapies for diseases mediated by superoxide radicals.

Original language	English (US)
Pages (from-to)	304-306
Number of pages	3
Journal	Science
Volume	286
Issue number	5438
DOIs	https://doi.org/10.1126/science.286.5438.304
State	Published - Oct 8 1999

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title = "A nonpeptidyl mimic of superoxide dismutase with therapeutic activity in rats",

abstract = "Many human diseases are associated with the overproduction of oxygen free radicals that inflict cell damage. A manganese(II) complex with a bis(cyclohexylpyridine)-substituted macrocyclic ligand (M40403) was designed to be a functional mimic of the superoxide dismutase (SOD) enzymes that normally remove these radicals. M40403 had high catalytic SOD activity and was chemically and biologically stable in vivo. Injection of M40403 into rat models of inflammation and ischemia-reperfusion injury protected the animals against tissue damage. Such mimics may result in better clinical therapies for diseases mediated by superoxide radicals.",

author = "Daniela Salvemini and Wang, {Zhi Qiang} and Zweier, {Jay L.} and Alexandre Samouilov and Heather Macarthur and Misko, {Thomas P.} and Currie, {Mark G.} and Salvatore Cuzzocrea and Sikorski, {James A.} and Riley, {Dennis P.}",

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doi = "10.1126/science.286.5438.304",

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T1 - A nonpeptidyl mimic of superoxide dismutase with therapeutic activity in rats

AU - Salvemini, Daniela

AU - Wang, Zhi Qiang

AU - Zweier, Jay L.

AU - Samouilov, Alexandre

AU - Macarthur, Heather

AU - Misko, Thomas P.

AU - Currie, Mark G.

AU - Cuzzocrea, Salvatore

AU - Sikorski, James A.

AU - Riley, Dennis P.

PY - 1999/10/8

Y1 - 1999/10/8

N2 - Many human diseases are associated with the overproduction of oxygen free radicals that inflict cell damage. A manganese(II) complex with a bis(cyclohexylpyridine)-substituted macrocyclic ligand (M40403) was designed to be a functional mimic of the superoxide dismutase (SOD) enzymes that normally remove these radicals. M40403 had high catalytic SOD activity and was chemically and biologically stable in vivo. Injection of M40403 into rat models of inflammation and ischemia-reperfusion injury protected the animals against tissue damage. Such mimics may result in better clinical therapies for diseases mediated by superoxide radicals.

AB - Many human diseases are associated with the overproduction of oxygen free radicals that inflict cell damage. A manganese(II) complex with a bis(cyclohexylpyridine)-substituted macrocyclic ligand (M40403) was designed to be a functional mimic of the superoxide dismutase (SOD) enzymes that normally remove these radicals. M40403 had high catalytic SOD activity and was chemically and biologically stable in vivo. Injection of M40403 into rat models of inflammation and ischemia-reperfusion injury protected the animals against tissue damage. Such mimics may result in better clinical therapies for diseases mediated by superoxide radicals.

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A nonpeptidyl mimic of superoxide dismutase with therapeutic activity in rats

Abstract

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