Table of Contents
Journal of Biophysics
Volume 2012, Article ID 606172, 14 pages
http://dx.doi.org/10.1155/2012/606172
Review Article

The Aggregation of Huntingtin and α-Synuclein

1Laboratorio de Patología Vascular Cerebral, Instituto Nacional de Neurología y Neurocirugía, Insurgentes sur 3877 Col. la Fama, 14269 Mexico, DF, Mexico
2Departamento de Ciencias Naturales, CNI, Universidad Autónoma Metropolitana Cuajimalpa, Pedro Antonio de los Santos 84 Col. Sn. Miguel Chapultepec Deleg, Miguel Hidalgo, 11851 México, DF, Mexico

Received 22 February 2012; Revised 15 May 2012; Accepted 17 May 2012

Academic Editor: Valeria Militello

Copyright © 2012 María Elena Chánez-Cárdenas and Edgar Vázquez-Contreras. 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.

Abstract

Huntington’s and Parkinson’s diseases are neurodegenerative disorders associated with unusual protein interactions. Although the origin and evolution of these diseases are completely different, characteristic deposits of protein aggregates (huntingtin and α-synuclein resp.), are a common feature in both diseases. After these observations, many studies are performed with both proteins. Some of them try to understand the nature and driving forces of the aggregation process; others try to find a correlation between the genetic and failure in protein function. Finally with the combination of both approaches, it was proposed that possible strategies deal with pathologic aggregation. Unfortunately, if protein aggregation is a cause or a consequence of the neurodegeneration observed in these pathologies, it is still debatable. This paper describes the process of aggregation of two proteins: huntingtin and α synuclein. The characteristics of the aggregation reaction of these proteins have been followed with novel methods both in vivo and in vitro; these studies include both the combination with other proteins and the presence of various chemical compounds. The ultimate goal of this study was to summarize recent findings on protein aggregation and its possible role as a therapeutic target in neurodegenerative diseases and their role in biomaterial science.