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|Title:||Influence of conformational antibodies on dissociation of fibrillar amyloid ß (Aß1-42) in vitro|
|Keywords:||Aggregation;Amyloid ß;Antibodies;ELISA;Fluorescence;Thioflavin T|
|Abstract:||Many neurodegenerative diseases result due to the accumulation of misfolded proteins as amyloid fibrils. Although the protein components of these fibrils from different disease states differ considerably, they appear to share common structure. Among these conformational disorders, Alzheimer’s disease (AD) and prion diseases exhibit significant overlap in their mechanism of pathogenesis. The present report demonstrates that antibodies directed against the prion protein repeat motif, Tyr-Tyr-Arg motif, recognize recombinantly expressed human amyloid ß (Aß) aggregates in enzyme linked immunosorbent assay. In addition, these antibodies dissociate the preformed aggregates of Aß in vitro. These findings illustrate an important property of conformation dependent antibodies viz., they specifically recognize the protein deposits associated with pathology and not the protein in normal tissue. These antibodies may benefit the development of approaches towards prevention and treatment of protein misfolding diseases.|
|Appears in Collections:||IJEB Vol.47(05) [May 2009]|
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