Next Article in Journal / Special Issue
Sirtuins and Proteolytic Systems: Implications for Pathogenesis of Synucleinopathies
Previous Article in Journal
The Role of Reactive Oxygen Species (ROS) in the Formation of Extracellular Traps (ETs) in Humans
Previous Article in Special Issue
Posttranslational Modifications and Clearing of α-Synuclein Aggregates in Yeast
Article Menu

Export Article

Open AccessArticle
Biomolecules 2015, 5(2), 724-734; doi:10.3390/biom5020724

Effects of Trehalose on Thermodynamic Properties of Alpha-synuclein Revealed through Synchrotron Radiation Circular Dichroism

1
Institute of Biomolecular Chemistry of CNR, Padua Unit, Padua 35131, Italy
2
Diamond Light Source Ltd., Harwell Innovation Campus, Chilton, Didcot, Oxfordshire OX11 0QX, UK
3
Department of Biology, University of Padua, Padua 35122, Italy
*
Author to whom correspondence should be addressed.
Academic Editor: Stephan N. Witt
Received: 13 March 2015 / Accepted: 16 April 2015 / Published: 4 May 2015
View Full-Text   |   Download PDF [142 KB, uploaded 4 May 2015]   |  

Abstract

Many neurodegenerative diseases, including Huntington’s, Alzheimer’s and Parkinson’s diseases, are characterized by protein misfolding and aggregation. The capability of trehalose to interfere with protein misfolding and aggregation has been recently evaluated by several research groups. In the present work, we studied, by means of synchrotron radiation circular dichroism (SRCD) spectroscopy, the dose-effect of trehalose on α-synuclein conformation and/or stability to probe the capability of this osmolyte to interfere with α-synuclein’s aggregation. Our study indicated that a low trehalose concentration stabilized α-synuclein folding much better than at high concentration by blocking in vitro α-synuclein’s polymerisation. These results suggested that trehalose could be associated with other drugs leading to a new approach for treating Parkinson’s and other brain-related diseases. View Full-Text
Keywords: trehalose; α-synuclein; synchrotron radiation circular dichroism (SRCD) spectroscopy; osmolytes trehalose; α-synuclein; synchrotron radiation circular dichroism (SRCD) spectroscopy; osmolytes
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Ruzza, P.; Hussain, R.; Biondi, B.; Calderan, A.; Tessari, I.; Bubacco, L.; Siligardi, G. Effects of Trehalose on Thermodynamic Properties of Alpha-synuclein Revealed through Synchrotron Radiation Circular Dichroism. Biomolecules 2015, 5, 724-734.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top