In-vitro Interaction of αB-Crystallin on Serum Amyloid a and Serum Amyloid a Fibrils with Neuro 2a Cells

The interactions of SAA and SAA protofibrils with protecting role of alphaB-Crystallin with neuro 2a cells of the mouse are dealt with in detail to study the binding of SAA protofibrils in various conditions. Specifically, interaction of serum amyloid A fibrils with a cell surface binding site/receptor might alter the local environment to cause cellular dysfunction and to be more favorable for amyloid formation and prevention. This is important in relation to the activity of membrane proteins, because losing the activity of such systems will ultimately lead to malfunction or death of the cell.  The interactions of Serum Amyloid A (SAA) and Serum Amyloid A protofibrils with neuro 2a cells of the mouse are dealt with in detail to study the binding of SAA protofibrils in various conditions. The induced fluorescence, induced circular dichroism, FACScan and MTT assay results have shown the SAA and SAA prototfibrils binding and cell toxicity with the neuro 2a cells with different concentrations of alphaB-Crystallin 0.15-15 nM. Specifically, cells were incubated with 1.25-6.25 mM SAA-FITC and SAA protofibrils-FITC assayed. The 50% viable neuro 2a cells at 4–6 mM with an LD₅₀ of 3.5 mM. The interaction of serum amyloid A fibrils with a cell surface binding site/receptor might alter the local environment to cause cellular dysfunction and to be more favorable for amyloid formation. In the present study, concluding that the SAA fibrils and SAA protein binding and neuro 2a cell cytotoxicity was reduced in the presence of alphaB-Crystallin.