The deposition of amyloid-β (Aβ) plaques in the brain is a significant pathological signature of Alzheimer’s disease, correlating with synaptic dysfunction and neurodegeneration. Several compounds, peptides, or drugs have been designed to redirect or stop Aβ aggregation. Among them, the trideca-peptide CWG-LRKLRKRLLR (mApoE), which is derived from the receptor binding sequence of apolipoprotein E, is effectively able to inhibit Aβ aggregation and to promote fibril disaggregation. Taking advantage of Atomic Force Microscopy (AFM) imaging and fluorescence techniques, we investigate if the clustering of mApoE on gold nanoparticles (AuNP) surface may affect its performance in controlling Aβ aggregation/disaggregation processes. The results showed that the ability of free mApoE to destroy preformed Aβ fibrils or to hinder the Aβ aggregation process is preserved after its clustering on AuNP. This allows the possibility to design multifunctional drug delivery systems with clustering of anti-amyloidogenic molecules on any NP surface without affecting their performance in controlling Aβ aggregation processes.

The clustering of mapoe anti-amyloidogenic peptide on nanoparticle surface does not alter its performance in controlling beta-amyloid aggregation

Corti R.;Nardo L.;Salerno D.;Re F.;
2020

Abstract

The deposition of amyloid-β (Aβ) plaques in the brain is a significant pathological signature of Alzheimer’s disease, correlating with synaptic dysfunction and neurodegeneration. Several compounds, peptides, or drugs have been designed to redirect or stop Aβ aggregation. Among them, the trideca-peptide CWG-LRKLRKRLLR (mApoE), which is derived from the receptor binding sequence of apolipoprotein E, is effectively able to inhibit Aβ aggregation and to promote fibril disaggregation. Taking advantage of Atomic Force Microscopy (AFM) imaging and fluorescence techniques, we investigate if the clustering of mApoE on gold nanoparticles (AuNP) surface may affect its performance in controlling Aβ aggregation/disaggregation processes. The results showed that the ability of free mApoE to destroy preformed Aβ fibrils or to hinder the Aβ aggregation process is preserved after its clustering on AuNP. This allows the possibility to design multifunctional drug delivery systems with clustering of anti-amyloidogenic molecules on any NP surface without affecting their performance in controlling Aβ aggregation processes.
AFM; Amyloid-β; Gold nanoparticles; MApoE; Alzheimer Disease; Amyloid; Amyloid beta-Peptides; Apolipoproteins E; Brain; Cluster Analysis; Gold; Humans; Metal Nanoparticles; Peptide Fragments; Plaque, Amyloid; Protein Binding
Corti, R.; Cox, A.; Cassina, V.; Nardo, L.; Salerno, D.; Marrano, C. A.; Missana, N.; Andreozzi, P.; Silva, P. J.; Stellacci, F.; Dal Magro, R.; Re, F.; Mantegazza, F.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11383/2133884
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