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Reviews in Analytical Chemistry

Editor-in-Chief: Schechter, Israel

Editorial Board: Pauw, Edwin / Vries, Mattanjah / Grushka, Eli / Laserna, J. / Licht, Stuart / Lubman, David / Mandler, Daniel / Palleschi, Vincenzo / Sigman, Michael / Whitesides, George


IMPACT FACTOR 2017: 2.111

CiteScore 2017: 1.67

SCImago Journal Rank (SJR) 2017: 0.505
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Volume 33, Issue 4

Issues

Synchrotron-based infrared spectroscopy brings to light the structure of protein aggregates in neurodegenerative diseases

Guylaine Hoffner
  • Corresponding author
  • Brain Physiology Laboratory, Centre National de la Recherche Scientifique, Paris Descartes University, 45 rue des Saints Pères, 75006 Paris, France
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ William André / Christophe Sandt / Philippe Djian
  • Corresponding author
  • Brain Physiology Laboratory, Centre National de la Recherche Scientifique, Paris Descartes University, 45 rue des Saints Pères, 75006 Paris, France
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2014-11-11 | DOI: https://doi.org/10.1515/revac-2014-0016

Abstract

The accumulation of misfolded proteins in the form of aggregates characterizes a number of diseases of the central nervous system such as Alzheimer’s disease, Parkinson’s disease, prion diseases, and the diseases of polyglutamine expansion. Recent evidence obtained in vitro and in mice has suggested that protein aggregates are structurally diverse and that their structure largely determines toxicity. The structure of the aggregated proteins in the brain of human patients remains mostly unknown, and we will give here the reasons for which synchrotron-based infrared spectroscopy is emerging as one of the best techniques to access this structure. We will also review the few publications that already exist on the application of synchrotron-based infrared spectroscopy to the study of protein aggregates in human brain. The establishment of a correlation between aggregate structure and neurological toxicity is important not only to understand the aggregation process itself but also in order to specifically target the most toxic structures when searching for prophylactic or therapeutic inhibitors of protein aggregation.

Keywords: Alzheimer; amyloid; Huntington; Parkinson; prion

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About the article

Guylaine Hoffner

Guylaine Hoffner obtained her PhD at the Denis Diderot University (Paris, France) on the study of the interaction of huntingtin with microtubules and its aggregation in Huntington disease. She worked as a postdoctoral fellow at Ecole Polytechnique (Palaiseau, France), where she developed a mass spectrometric method for the quantification of a potential biomarker in neurological diseases. She is now an INSERM research scientist working at the Paris Descartes University (France), where she studies protein aggregation in Huntington disease by biochemical and biophysical techniques.

William André

William André obtained his PhD from Université Paris Descartes in 2012. He studied the structural polymorphism of the protein aggregates associated with Huntington’s disease. He also characterized the substrates of cerebral transglutaminase, which are Ca2+-dependent enzymes possibly involved in Huntington’s disease. He now holds a postdoctoral position at SOLEIL synchrotron on the infrared beam line, where he studies the effect of the cellular environment on the development of pulmonary arterial hypertension.

Christophe Sandt

Christophe Sandt holds a PhD in biophysics from the Reims University, France, on the identification of pathogenic microorganisms by FTIR microspectroscopy. He worked as a postdoc in the Chemistry Department of Montréal and of Saint Francis Xavier Universities, Canada, on the penetration of biocides in bacterial biofilms by FTIR-ATR spectroscopy and FTIR imaging and on bacterial biofilms composition using Raman microspectroscopy. He is now a scientist at the infrared beamline SMIS at synchrotron SOLEIL, and his main line of work is developing FTIR microspectroscopy for cellular biology applications.

Philippe Djian

Philippe Djian obtained an MD degree from the Université de Nice, France. He was a postdoctoral fellow in the department of Cell Biology at Harvard Medical School. He then became Directeur de Recherche at the CNRS in Paris. He was director of the Neuroscience Institute and of the laboratory of genetic regulation and genetic diseases at the Université Paris Descartes from 2000 to 2013. His research interests include diseases of polyglutamine expansion and the study of zinc finger proteins in development.


Corresponding authors: Guylaine Hoffner and Philippe Djian, Brain Physiology Laboratory, Centre National de la Recherche Scientifique, Paris Descartes University, 45 rue des Saints Pères, 75006 Paris, France, e-mail: ;


Received: 2014-06-03

Accepted: 2014-10-12

Published Online: 2014-11-11

Published in Print: 2014-12-01


Citation Information: Reviews in Analytical Chemistry, Volume 33, Issue 4, Pages 231–243, ISSN (Online) 2191-0189, ISSN (Print) 0793-0135, DOI: https://doi.org/10.1515/revac-2014-0016.

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