Scientists of the Department of Physical Chemistry of the Universidad de Granada are doing research into the molecular basis which provoke the formation of “amyloid fibres” from a model protein and causing certain degenerative diseases of the nervous system such as Alzheimer, el Parkinson or the “mad cow disease”, both in animals and humans, as well as other non-neurological pathologies like type 2 diabetes or certain disorders connected with haemodialysis. These disorders are characterized by the uncontrolled formation protein deposits in amyloid deposits in tissues and organs, altering their operation.
Francisco Conejero Lara, researcher in charge of the project, has explained that the better they get to know the mechanism and the characteristics of the formation process of these fibres, the sooner they will be able to intervene through drugs preventing or postponing the fibre deposit. This way it will be possible to prevent or reduce the damage provoked by such process in the affected organs.
Due to different factors, many of which are to be determined, it is possible to favour an abnormal protein folding to a conformation that determines and starts the formation of amyloid fibres. In the intermediate phases of the process there is a build-up of “sticky” structures which, according to the researcher, are the precursors of these protein “additions”.
In the previously mentioned diseases, they have observed that regardless of the responsible proteins, all of them settle forming a common structure, consisting on an enormous “B sheet” which extends uninterruptedly all through the fibre. In addition, according to the scientists, different proteins, many of them even without any connection with amyloid diseases, can form the same fibres with the same aspect –at the microscope- and structure if they are subjected to the appropriate conditions.
Src homology 3
The researchers from Granada are working with a Src homology 3. It is a protein fragment which, although it is not connected with the formation of deposits in degenerative diseases, is capable of forming these fibres. From the “in vitro” experimentation, the scientists are studying the molecular basis causing an irregular protein folding. To this extent, they have focused on the characterizing the stability, structure and factors (kinetic and thermodynamic) of the precursors of the formation of Src homology 3 amyloid fibres.
The scientists are collaborating with seven European laboratories, aimed at finding common characteristics that allow to establish a general mechanism for the formation of the amyloid fibres.
Reference:
Prof Francisco Conejero Lara. Department of Physical Chemistry.
Phone number: 958 242 371 / 243331.
E-mail: conejero@ugr.es
