Table 3.

Aβ-nanoparticle interaction.

Nanomaterials class	Nanomaterials name	Nanomaterials properties	Peptide	Biological effect	Effect on amyloidosis	Mode of interaction	Year	Ref.
Inorganic nanomaterials	Nanoceria	Size: 3–8 nm	Aβ25–35	•Accumulate at mitochondrial outer membrane and plasma membrane •Reduce mitochondrial fragmentation •Reduce neuronal cell death		Block Aβ-mediated mitochondrial fragmentation via the reduction of DRP1 S616 hyperphosphorylation	2014	[157]
	SPIONs-PEG-NH2	Size: 20 nm Surface charge: 17.4 ± 2.5 mV	Aβ42		Dual effects on Aβ fibrillization: •High concentrations accelerate fibrillization under magnetic field •Lower concentrations inhibit fibrillization under magnetic field	Magnetic field on the size and surface charge of SPIONs, thereby impacting Aβ fibrillization	2015	[156]
	AuNPs	Size: 20, 50 and 80 nm	Aβ	Aβ oligomers more toxic than Aβ fibrils or plaques in inducing acute cell death	•Aβ aggregates on nanoparticle surfaces •Larger particles induce more Aβ aggregation on particle surfaces with a shortened lag phase		2015	[149]
		Surface charge: positive (amine-AuNPs), negative (citrate-AuNPs)	Aβ		•Amine-AuNPs are more strongly attracted to Aβ, forming smaller aggregates, not protofibrils •Citrate-AuNPs act as nucleation seeds to accelerate fibrillization	•Electrostatic interactions •Replacement of citrate on AuNPs with Aβ and direct attachment of AuNPs to Aβ
		Shape: Spherical AuNPs, nanorods (AuNRs), and nanocubes (AuNCs)	Aβ	Nanostructure-dependent cytotoxicity on neuroblastoma cells	•AuNCs interact with Aβ to produce fibril networks •AuNRs inhibit Aβ aggregation	•AuNCs possess a larger effective surface area and are more isotropic than AuNRs •Larger aggregates form on AuNCs
	CeONP@POMs	Size: ~5 nm Surface charge: −48.2 mV	Aβ40	•Reduce intracellular ROS •Promote PC12 cell proliferation •Cross the BBB •Inhibit Aβ-induced BV2 microglial cell activation	•Inhibit Aβ fibrillization •Disaggregate peptide fibrils •Hydrolyze peptide monomers	Hydrolytic effect	2016	[151]
	MoS2 NPs	Size: ~100 nm FTIR peaks: 1630, 1420, and 1280 cm−1	Aβ42	•Scavenge ROS •Block formation of Ca2+ channel in cell membrane •Alleviate cell toxicity	•Inhibit Aβ fibrillization •Destabilize Aβ fibrils	Electrostatic attraction and high surface ratio effects	2017	[150]
	CGA@SeNPs	Size: ~100 nm	Aβ40	•Reduce ROS generation •Inhibit neurotoxicity of Aβ40	Inhibit Aβ aggregation	Aβ binds on SeNPs via N-donors containing side chains of amino acids to form an Se–N bond, blocking direct contact between peptide monomers	2018	[155]
	βCas AuNPs	Size: 7.5 ± 2.6 nm Surface charge: −11.7 ± 1.8 mV	Aβ42	•No lethality but reduced locomotion, nonresponsive mobility and a loss of balance in larvae upon Aβ injection •βCas AuNPs recover the mobility and cognitive function of adult zebrafish	•No such mitigation is obtained with caseins alone •βCas promote fast Aβ nucleation	Sequester toxic Aβ42 through a nonspecific, chaperone-like manner	2019	[24]
	SiO2–cyclen	Size: 65.2 ± 4.9 nm	Aβ40	•Cross the BBB •Reduce cytotoxicity and ROS	Inhibit metal-induced aggregation (Zn2+, Cu2+)	•Metal-chelation •Crossing the BBB via adsorptive or receptor-mediated transportation	2019	[154]
	BP@BTA	Height: 3–5 nm UV–vis: 345 nm (BTA, covalent interaction with BP)	Aβ42	•Reduce the peptide cytotoxicity •Attenuate peptide neurotoxicity to CL2006, extend the lifespan of worms •BP@BTA and its degradation products are nontoxic and biocompatible	•Inhibit Aβ aggregation under NIR, no effect under dark •Oxygenate Aβ	High affinity for Aβ due to specific amyloid selectivity of BTA	2019	[153]
	AgTNPs	Edge length: 70 ± 8 nm Surface charge: −41 ± 1.4 mV	Aβ40	Increase cell viability	•Prevent formation of Aβ fibrils •Dissolve mature Aβ fibrils	•AgTNPs selective bind the positively charged amyloidogenic sequence of Aβ monomer •AgTNPs dissolve mature Aβ fibrils via plasmonic photothermal property	2019	[152]
Polymeric nanomaterials	PMA-nanodiscs	Size: ~10 nm	Aβ40	Aβ40 oligomers incubated with PMA-nanodiscs exhibit relatively less neurotoxic and neuronal damage	•Lipid concentration and composition are important to regulate Aβ fibrillization •Form low-ordered Aβ aggregates in the presence of nanodiscs	Amide (H–N) and side chain protons of Aβ show a correlation with PMA functional groups, hydrophobic chain and quaternary ammonium group	2018	[159]
	NC-KLVFF	Size: 14 ± 4 nm	Aβ42	•Attenuate neuron damage •Regain endocranial microglia’s capability to phagocytose Aβ •Protect hippocampal neurons against Apoptosis	•Inhibit self-aggregation of Aβ •Dissociate Aβ fibrils	•Polymeric surface property impacts peptide binding affinity •Block interaction between Aβ oligomers and cell membranes	2019	[22]
	CPNPs	Size: ~4.7 nm Surface charge: ~ 30 mV	Aβ40		Inhibit Aβ fibrillization	Binding to the termini of seed fibrils can effectively inhibit fibrillization	2019	[165]
	G5-PAMAM G6-PAMAM	NMR: 7.05–7.25 ppm UV peak: 260 nm	Aβ42		Phenyl derivatives of high-generation dendrimers (G5-P and G6-P) significantly inhibit Aβ42 aggregation and alter ultrastructure of Aβ42 aggregates	Hydrophobic binding-electrostatic repulsion theory	2019	[160]
Carbon-based nanomaterials	GQDs	Size: ~8 nm Surface charge: negative	Aβ42	•Increase survival rate •Great biocompatibility	Inhibit Aβ fibrillization	Hydrophobic and electrostatic interactions	2015	[166]
	C60(OH)16		Aβ40	Biocompatible materials	•Reduce the formation of amyloid fibrils	•Electrostatic interactions •Binding with hydrophobic Aβ C-terminus	2016	[167]
	SWNT-OH	Size: ~8 nm	Aβ42	Cytoprotective effects against Aβ42 fibrillization-induced cytotoxicity	•Inhibit Aβ42 fibrillization •Disaggregate preformed amyloid fibrils	Nonpolar interactions, especially van der Waals forces	2019	[168]
	CQDs	Size: ~2.8 nm Surface charge: ~−44.6 mV	Aβ42	Restore embryo survival rate by 32% Decrease ROS production	Inhibit Aβ fibrillization	Hydrophobic interaction and H-bonding	2020	[138]
Biologically inspired nanomaterials	ApoE3-rHDL nanodiscs	Size: 27.9 ± 8.9 nm Surface charge: −4.07 ± 0.83 mV	Aβ40, Aβ42	•Accelerate microglial, astroglial, and liver cell degradation of Aβ by facilitating lysosomal transport •Cross the BBB	Inhibit Aβ aggregation	•Receptor-mediated endocytosis •High binding affinity for Aβ monomers and oligomers	2014	[162]
	αNAP-GM1-rHDL	Size: 25.42 ± 1.18 nm Surface charge: −15.70 ± 0.93 mV	Aβ42	•Decrease cell toxicity in vitro •Reduce Aβ deposition, ameliorate neurologic changes, and rescue memory loss in vivo	•Inhibit Aβ aggregation •High Aβ binding affinity and clearance activity	•Aβ targeting: GM1 •ApoE-concentration-dependent binding synergetic effect of DMPC, GM1 and ApoE	2015	[163]
	ANC-α-M	Size: 35.95 ± 9.05 nm Surface charge: negative	Aβ42	•Accelerate Aβ42 degradation •Facilitate microglia-mediated uptake in vitro •Decrease amyloid deposition, attenuate microgliosis, and rescue memory deficit in AD mice	Block formation of both Aβ oligomers and fibrils, disturb preformed fibrils	•High affinity for Aβ monomers and oligomers •ApoE-dependent cellular uptake	2016	[161]
	dcHGT NPs	Size: ~15 nm	Aβ42	•Relieve inflammation and protect primary neurons from Aβ oligomer-induced neurotoxicity in vitro •Reduce Aβ deposition, ameliorate neuron morphological changes, rescue memory deficits, and improve acetylcholine regulation ability in vivo	Inhibit and eliminate Aβ aggregation	•Aβ targeting-GM 1 •Metal-ion chelation and inhibition of AChE activity	2020	[164]