Misfolded Protein Diagnostic Detects Amyloid Neurologic Diseases

A study examined the ability of the misfolded protein diagnostic (MPD) assay to detect the presence of misfolded proteins in brain, serum, and plasma.

The investigators demonstrated that the MPD assay is a sensitive and specific test for the detection misfolded prion proteins. This will help both preclinical and clinical diagnosis of transmissible spongiform encephalopathy (TSE) diseases in both animals and humans. The results of the study appeared in the August 2007 issue of the journal Transfusion.

Scientists have tried to develop a preclinical diagnostic test for TSE since the discovery that humans with variant Creutzfeldt-Jakob disease can transmit disease via blood transfusions. However, there are several challenges to detecting misfolded proteins in the blood such as the coexistence of a large amount of the protein in its normally folded shape, and the fact that misfolded proteins do not trigger an immune system response that would enable diagnosis based on the detection of antibodies. In addition, most standard detection methods are not sensitive enough to detect the low level of misfolded proteins in the blood, especially during early disease stages. These challenges have largely restricted diagnostic tests for such amyloid diseases to the use of postmortem tissue.

The MPD assay, developed by Adlyfe (Rockville, Maryland, USA), is based on the synthesis of conformationally sensitive peptides, which are created to target specific protein shapes associated with various diseases. The interaction of the target protein with Adlyfe's proprietary peptides produces a conformational change that transduces a fluorescent signal. Further amplification of the signal is generated as additional ligands undergo conformational changes. This is the basis for the test's sensitivity and its ability to detect very low amyloid protein levels before symptoms occur.

"The publication of this study validates the utility and sensitivity of our MPD assay in detecting misfolded proteins in TSE, even at low levels,” said Adlyfe CEO Alan S. Rudolph, Ph.D. "We believe our test meets the dual diagnostic demands of confirmatory testing in symptomatic subjects suspected of having the disease and as a screening test to identify infection in its earliest phases. Our unique diagnostic approach and technology is applicable to a number of neurological diseases associated with protein buildup in tissues such as Creutzfeldt-Jakob disease [CJD], Alzheimer's, and Parkinson disease.”


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