UNC scientists conducted studies on the structure of potentially toxic protein aggregates in disease. It is an important contribution.
The whole MRIA Soledad (39) and Jose Ignacio Gallea (28) they are two scientists Cordoba, National University of Cordoba (UNC) investigating at the Faculty of Chemistry, for some years, how proteins involved in Parkinson interrelate, a disease that affects the world some six million people and, in Argentina, a cerca de 70 one thousand.
The studies, recently published in the scientific journal Journal of Biological Chemistry ( JBC ), They are a contribution to the study of this disease, from basic science, biophysics and molecular biology. That is, it is another piece in the puzzle of understanding the mechanism operating in these pathologies. The investigation, also, It can serve for the eventual development of drugs.
The research is part of the doctoral thesis Gallea, Fellow CONICET, whose thesis supervisor is Celej, CONICET researcher and professor at the School of Chemical Sciences of the UNC. Both work in the area of Biophysics in the Department of Biological Chemistry (Ciquibic).
The scientists studied the acquisition of abnormal protein structures linked to Parkinson. Celej said, to fulfill its role, proteins have to adopt a particular structure or three-dimensional shape, must be folded.
"When there is a problem of folding, Cell has tools to try to correct the misfolding. When a protein can not take this three-dimensional array, Cell degrades, trying to get rid of it ", Indian. When not happen and start to accumulate these misfolded proteins are known as diseases that are generated agregopatías, many are neurodegenerative, such as Alzheimer's, The "mad cow" or Parkinson.
"The protein we work is linked to the pathology of Parkinson, It is the alpha synuclein protein ", said Celej, one of the researchers listed in the list of scientific repatriated. He returned to Germany in 2008.
In research, It held by national funds and some international contributions, structural aspects were studied in vitro .
"We knew that in this three-dimensional array with proteins there are different ways. Some are and some are tape-type propeller type. We knew that these species prefibrilar added protein are called oligomers are partly shaped structure with an antiparallel arrangement tapes. Some have an orientation and other, other. But we did not know what regions of the proteins could be interrelated with each other in these aggregates prefibrilares, that they are more toxic in these diseases, not only in Parkinson ", He remarked Celej.
Valuable information
During a mapping of proteins was performed. "For these diseases do not actually know what the mechanism of action, why they would be dying cells in those regions of the brain and how it works. It is this type of fibrillar protein aggregates but not really know why add ", said Gallea. He added: "The novelty is that we provide structural information of these potentially toxic aggregates prefibrilares".
Research in specific regions postulated protein which would be established interactions, which would be key to bringing the eventual development of specific medication information. "We identified particular regions. That's new. Until now it was not known ", say researchers.
The work was published in JBC , Founded in 1905 by the American Society for Biochemistry and Molecular Biology.
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