A ccumulation of beta-amyloid(A beta) fibrils in the brain is one of the main culprits in Alzheimer's disease(AD) progression, which initiates the neuronal damage and subsequent neurodegeneration. Various anti-A beta agents have shown the potentials to dissociate A beta fibrils. However, these approaches can't facilitate the removal of A beta fibrils, resulting in a disappointing therapeutic effect. Herein, we demonstrate an integrated polymer nanocomposite(NP-GLVFF-IgG) that can dissociate A beta fibrils into fragments and activate microglia to remove the fragments via Fc receptors-mediated phagocytosis. NP-GLVFF-IgG is constructed by an albumin/polymer hybrid nanoparticle with Gl gamma-Leu-Val-Phe-Phe (GLVFF) peptides and Immunoglobulin G(IgG) molecules on the surface. In this design, NP-GLVFF-IgG achieves to dissociate the A beta fibrils by the strong hydrogen-bonding interactions between A beta fibrils and GLVFF peptides. Then, NP-GLVFF-IgG activates the microglial phagocytosis, thereby achieving an enhanced phagocytic removal of A beta fibrils for neuroprotection. Moreover, NP-GLVFF-IgG achieves to trigger the effective removal of A beta fibrils even under inflammatory condition that usually suppressed phagocytosis. Therefore, NP-GLVFF-IgG has great potential as a novel therapeutic platform for effective AD therapy.