XML Feed for RxPG News   Add RxPG News Headlines to My Yahoo!   Javascript Syndication for RxPG News

Research Health World General
 
  Home
 
 Latest Research
 Cancer
 Psychiatry
 Genetics
 Surgery
 Aging
 Ophthalmology
 Gynaecology
 Neurosciences
  Memory
  Regeneration
  Stroke
  Brain Diseases
  Headache
  Spinal Cord Diseases
  Demyelinating Diseases
  Neurodegenerative Diseases
   Rett Syndrome
  Taste
  Trigeminal Neuralgia
 Pharmacology
 Cardiology
 Obstetrics
 Infectious Diseases
 Respiratory Medicine
 Pathology
 Endocrinology
 Immunology
 Nephrology
 Gastroenterology
 Biotechnology
 Radiology
 Dermatology
 Microbiology
 Haematology
 Dental
 ENT
 Environment
 Embryology
 Orthopedics
 Metabolism
 Anaethesia
 Paediatrics
 Public Health
 Urology
 Musculoskeletal
 Clinical Trials
 Physiology
 Biochemistry
 Cytology
 Traumatology
 Rheumatology
 
 Medical News
 Health
 Opinion
 Healthcare
 Professionals
 Launch
 Awards & Prizes
 
 Careers
 Medical
 Nursing
 Dental
 
 Special Topics
 Euthanasia
 Ethics
 Evolution
 Odd Medical News
 Feature
 
 World News
 Tsunami
 Epidemics
 Climate
 Business
Search

Last Updated: Aug 19th, 2006 - 22:18:38
Breakthrough

Neurodegenerative Diseases Channel
subscribe to Neurodegenerative Diseases newsletter

Latest Research : Neurosciences : Neurodegenerative Diseases

   DISCUSS   |   EMAIL   |   PRINT
Discovery may improve treatment of neurodegenerative diseases
Dec 15, 2005, 16:14, Reviewed by: Dr. Sanjukta Acharya

"This 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"

 
A team of scientists from the Universitat Autňnoma 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 fibres. 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 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.

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 fibres. 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.

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".

Globular protein


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 stabilising the structure of the protein, while preventing the "hot spots" from becoming exposed.
 

- BMC Structural Biology
 

www.uab.es

 
Subscribe to Neurodegenerative Diseases Newsletter
E-mail Address:

 

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 Autňnoma de Barcelona.

Related Neurodegenerative Diseases News

3-D forms link antibiotic resistance and pantothenate kinase associated neurodegeneration
New biomarkers could help doctors spot neurodegenerative diseases
Nitration Linked to Oxidative Stress Related Damage in Neurodegenerative Disorders
REM sleep disorders can indicate early neurodegeneration
Neurodenegerative diseases mechanisms linked to transport proteins
New Tools Developed for Studying Neurodegenerative Brain Disorders
New Tools Developed for Studying Neurodegenerative Brain Disorders
Research Suggests Abraham Lincoln Suffered from Spinocerebellar Ataxia type 5 (SCA5)
Discovery may improve treatment of neurodegenerative diseases
Possible molecular origin of nervous system degeneration diseases


For any corrections of factual information, to contact the editors or to send any medical news or health news press releases, use feedback form

Top of Page

 

© Copyright 2004 onwards by RxPG Medical Solutions Private Limited
Contact Us