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Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126. / Turnbull, Stuart; Tabner, Brian J.; Brown, David R. et al.
In: NeuroReport, Vol. 14, No. 13, 15.09.2003, p. 1743-1745.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Turnbull, S, Tabner, BJ, Brown, DR & Allsop, D 2003, 'Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126.', NeuroReport, vol. 14, no. 13, pp. 1743-1745. <http://www.neuroreport.com/pt/re/neuroreport/abstract.00001756-200309150-00017.htm;jsessionid=Lq2JgG81V7vkQYBSLqgGpT4TfPyHvkqTnjvNCFQ8Xfj2nrKm3794!298990308!181195629!8091!-1>

APA

Turnbull, S., Tabner, B. J., Brown, D. R., & Allsop, D. (2003). Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126. NeuroReport, 14(13), 1743-1745. http://www.neuroreport.com/pt/re/neuroreport/abstract.00001756-200309150-00017.htm;jsessionid=Lq2JgG81V7vkQYBSLqgGpT4TfPyHvkqTnjvNCFQ8Xfj2nrKm3794!298990308!181195629!8091!-1

Vancouver

Turnbull S, Tabner BJ, Brown DR, Allsop D. Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126. NeuroReport. 2003 Sept 15;14(13):1743-1745.

Author

Turnbull, Stuart ; Tabner, Brian J. ; Brown, David R. et al. / Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126. In: NeuroReport. 2003 ; Vol. 14, No. 13. pp. 1743-1745.

Bibtex

@article{9f8e5ac7779545af8c027503e9b4ee9f,
title = "Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126.",
abstract = "The accumulation of protein aggregates in the brain is a central feature of several different neurodegenerative diseases. We have recently shown that A[beta] and [alpha]-synuclein, associated with Alzheimer's disease, Parkinson's disease and related disorders, can both induce the formation of hydroxyl radicals following incubation in solution, upon addition of Fe(II). PrP106-126, a model peptide for the study of prion protein-mediated cell death, shares the same property. In this study we show that quinacrine (an anti-malarial drug and inhibitor of prion replication) acts as an effective antioxidant, readily scavenging hydroxyl radicals formed from hydrogen peroxide via the Fenton reaction or generated during incubation of the PrP106-126 peptide. Furthermore, the toxicity of PrP106-126 to cultured cells was significantly inhibited by quinacrine.",
author = "Stuart Turnbull and Tabner, {Brian J.} and Brown, {David R.} and David Allsop",
year = "2003",
month = sep,
day = "15",
language = "English",
volume = "14",
pages = "1743--1745",
journal = "NeuroReport",
issn = "1473-558X",
publisher = "LIPPINCOTT WILLIAMS & WILKINS",
number = "13",

}

RIS

TY - JOUR

T1 - Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126.

AU - Turnbull, Stuart

AU - Tabner, Brian J.

AU - Brown, David R.

AU - Allsop, David

PY - 2003/9/15

Y1 - 2003/9/15

N2 - The accumulation of protein aggregates in the brain is a central feature of several different neurodegenerative diseases. We have recently shown that A[beta] and [alpha]-synuclein, associated with Alzheimer's disease, Parkinson's disease and related disorders, can both induce the formation of hydroxyl radicals following incubation in solution, upon addition of Fe(II). PrP106-126, a model peptide for the study of prion protein-mediated cell death, shares the same property. In this study we show that quinacrine (an anti-malarial drug and inhibitor of prion replication) acts as an effective antioxidant, readily scavenging hydroxyl radicals formed from hydrogen peroxide via the Fenton reaction or generated during incubation of the PrP106-126 peptide. Furthermore, the toxicity of PrP106-126 to cultured cells was significantly inhibited by quinacrine.

AB - The accumulation of protein aggregates in the brain is a central feature of several different neurodegenerative diseases. We have recently shown that A[beta] and [alpha]-synuclein, associated with Alzheimer's disease, Parkinson's disease and related disorders, can both induce the formation of hydroxyl radicals following incubation in solution, upon addition of Fe(II). PrP106-126, a model peptide for the study of prion protein-mediated cell death, shares the same property. In this study we show that quinacrine (an anti-malarial drug and inhibitor of prion replication) acts as an effective antioxidant, readily scavenging hydroxyl radicals formed from hydrogen peroxide via the Fenton reaction or generated during incubation of the PrP106-126 peptide. Furthermore, the toxicity of PrP106-126 to cultured cells was significantly inhibited by quinacrine.

M3 - Journal article

VL - 14

SP - 1743

EP - 1745

JO - NeuroReport

JF - NeuroReport

SN - 1473-558X

IS - 13

ER -