Anesthetic XXXX induces amyloidogenesis and cytotoxicity in human serum albumin.

@entity3884 @entity6635 @entity39 @entity33270 @entity23054 @entity7732
@entity23054 ( @entity33270 ) mimics the membrane environments as it simulates the hydrophobic environment and better stabilizes the secondary structures in peptides owing to its hydrophobicity and @entity3884 bond-forming properties. Its dielectric constant approximates that of the interior of proteins and is one-third of that of water. Human serum albumin (HSA) is a biological transporter. The effect of @entity33270 on HSA gives the clue about the conformational changes taking place in HSA on transport of ligands across the biological membranes. At 25% (v/v) and 60% (v/v) @entity33270 , HSA exhibits non-native b-sheet, altered @entity6635 fluorescence, exposed hydrophobic clusters, increased @entity7732 fluorescence and prominent red shifted Congo red absorbance, and large hydrodynamic radii suggesting the aggregate formation. Isothermal titration calorimetric results indicate weak binding of @entity33270 and HSA. This suggests that solvent-mediated effects dominate the interaction of @entity33270 and HSA. TEM confirmed prefibrillar at 25% (v/v) and fibrillar aggregates at 60% (v/v) @entity33270 . Comet assay of prefibrillar aggregates showed DNA damage causing cell @entity39 hence confirming cytotoxic nature. On increasing concentration of @entity33270 to 80% (v/v), HSA showed retention of native-like secondary structure, increased Trp and ANS fluorescence, a transition from b-sheet to a-helix. Thus, @entity33270 at high concentration possess anti- aggregating potency.
