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Adlyfe Study on the Detection of Misfolded Proteins Published in the Journal Transfusion
Date:8/29/2007

nology is based on the synthesis of conformationally sensitive peptides (chains of amino acids that are smaller than proteins) 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 tests' sensitivity and 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 Chief Executive Officer 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."

About Adlyfe

Adlyfe Inc. was established early in 2003 to develop novel technologies for blood testing for early targets of amyloid diseases. Adlyfe is developing a novel test for the detection and amplification of amyloid proteins as early biomarkers of fatal brain and amyloid diseases such as Alzheimer's disease, Parkinson's disease, Creutzfeldt-Jacob disease, Huntington's disease, systemic amyloidosis, diabetes and other diseases.

The Company's novel technology is based on the synthesis of small peptide, or Pronucleon(TM) ligands, that are amino acid sequence matched to target amyloids of interest. Ligand sequences are selected based on regions of the target protein known to undergo conformational changes (structural changes in shape) associated with amyloid
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