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Drug Targets Misfolded Protein Diseases

 
  May, 16 2002 0:44
your information resource in human molecular genetics
 
     
In this week's Nature (Vol. 417, No. 6886, 16 May 02, pp. 254-259), researchers reveal a drug that could erode the protein clumps plaguing sufferers of human amyloid diseases including Alzheimer's and type II diabetes.

In these disorders, normally soluble proteins fold abnormally and are laid down as insoluble fibrils that damage tissue. A second protein, called serum amyloid P component (SAP), binds fibrils and makes them particularly resistant to breakdown by the body.

Mark Pepys of the Royal Free and University College Medical School in London and colleagues have identified a compound that prevents SAP binding. The compound blocks SAP's attachment site and accelerates SAP degradation by the liver. Amyloid deposits in animal models were reduced by administration of the drug.

Initial studies have already been carried out on patients suffering systemic amyloidosis, a rare condition in which widespread amyloid deposits are ultimately fatal. The drug drained the stabilizing protein from amyloid clumps: "It's doing an incredible vanishing trick," says Pepys.

Pepys is shortly embarking on clinical trials for Alzheimer's sufferers. "This new approach offers great promise," comments Leslie Iversen of the Wolfson Centre for Age Related Diseases, King's College, London in an associated News and Views article.

CONTACT:

Mark Pepys
tel +44 207 433 2801
e-mail m.pepys@rfc.ucl.ac.uk

Leslie Iversen
tel (currently at) +44 1865 271 634
e-mail les.iversen@pharmacolgy.oxford.ac.uk

(C) Nature press release.


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