Covalent immobilization of human serum albumin on cellulose acetate membrane for scavenging amyloid beta - A stepping extracorporeal strategy for ameliorating Alzheimer's disease

Alzheimer's disease (AD) is a neurodegenerative disorder characterized by interrupted neurocognitive functions and impaired mental development presumably caused by the accumulation of amyloid beta (Aβ) in the form of plaques. Targeting Aβ has been considered a promising approach for treating AD. In the current study, human serum albumin (HSA), a natural Aβ binder, is covalently immobilized onto the surface of a cellulose acetate (CA) membrane to devise an extracorporeal Aβ sequester. The immobilization of HSA at 3.06 ± 0.22 μg/mm² of the CA membrane was found to be active functionally, as evidenced by the esterase-like activity converting p-nitrophenyl acetate into p-nitrophenol. The green fluorescent protein-Aβ (GFP-Aβ) fusion protein, recombinantly produced as a model ligand, exhibited characteristics of native Aβ. These features include the propensity to form aggregates or fibrils and an affinity for HSA with a dissociation constant (K_D) of 0.91 μM. The HSA on the CA membrane showed concentration-dependent sequestration of GFP-Aβ in the 1-10-μM range. Moreover, it had a greater binding capacity than HSA immobilized on a commercial amine-binding plate. Results suggest that the covalent immobilization of HSA on the CA surface can be used as a potential platform for sequestering Aβ to alleviate AD.