New Discovery Improves Treatment of Neurodegenerative Diseases and Type 2 Diabet

New Discovery Improves Treatment of Neurodegenerative Diseases and Type 2 Diabetes

New method is able to identify the precise zones of each protein that force the proteins to bond, aggregate and form amyloid fibers. New method very useful for designing new drugs to prevent the protein aggregation.

Proteins are large molecular chains that move around cells carrying vital information on the activity of the organism. The role of each protein depends largely on the form it takes, but the proteins occasionally lose this form when they collide and bind with other proteins.

They aggregate, and lose their function, growing continuously to form what are known as amyloid fibers. This causes neurodegenerative diseases, such as Parkinson’s, Alzheimer’s, and forms of spongiform encephalopathy, such as mad cow disease (BSE) and its human form, Creuzfeldt-Jacob disease. It also produces the pancreatic malfunctions that cause type 2 diabetes.

A team of scientists from the Universitat de Barcelona, led by the researcher Salvador Ventura, has developed a method that allows those parts of the proteins that set off aggregation to be identified. Using this method one is able to identify the precise zones of each protein that force these proteins to bond, aggregate and form amyloid fibers. The scientists have tested the method with different proteins involved in conformational diseases, while identifying zones that were already known for their role in protein aggregation and the diseases mentioned above.

According to Salvador Ventura, their method “identifies potential therapeutic targets against illnesses caused by protein aggregation, such as Alzheimer’s, Parkinson’s and type 2 diabetes. It allows a more precise identification of the targets, meaning that in theory they can be attacked more effectively”.

The method created by the UAB researchers identifies the “hot spots” that cause protein aggregation both in globular proteins, which are folded chains, and in unfolded chains. This method may be extremely useful for designing new drugs to fight illnesses related to protein aggregation. For unfolded chains, the method can be used to design drugs that act by completely covering and shielding the “hot spots” identified through the new method so that they cannot come into contact with other proteins and aggregate. If the proteins are globular, the aggregation “hot spots” are usually protected on the inside, and are not dangerous unless they are accidentally exposed to the outside. In this case the drugs must be aimed at stabilizing the structure of the protein, while preventing the “hot spots” from becoming exposed.

The research, recently published in BMC Structural Biology, was carried out by Natalia Sánchez de Groot, Irantzu Pallarés, Francesc Xavier Avilés, Josep Vendrell and Salvador Ventura, of the Department of Biochemistry and Molecular Biology and the Institute of Biotechnology and Biomedicine (IBB) at the Universitat Aut?a de Barcelona

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DID YOU KNOW: Restless legs syndrome (RLS) is common in type 2 diabetes. It is a neurological condition characterized by unpleasant sensations deep inside in the legs that occur at rest, especially at bedtime. The quality of sleep and the presence of RLS in a group of patients with type 2 diabetes have been studied. RLS was found to be present in almost one-third of the patients, and poor sleep quality was present in almost half of the patients. Treatment with dopaminergic agents, opioids, benzodiazepines, or anticonvulsant drugs has been reported to improve somatic complaints and sleep parameters. Diabetes Care,28 (2633-2636): Lopes L, de MM Lins C, Adeodato V, Quental D, de Bruin P, Montenegro R Jr, de Bruin V Restless legs syndrome and quality of sleep in type 2 diabetes