Adsorption and decontamination of α-synuclein from medically and environmentally-relevant surfaces

Abstract

The assembly and accumulation of α-synuclein fibrils are implicated in the development of several neurodegenerative disorders including multiple system atrophy and Parkinson's disease. Pre-existing α-synuclein fibrils can recruit and convert soluble non-fibrillar α-synuclein to the fibrillar form similar to what is observed in prion diseases. This raises concerns regarding attachment of fibrillary α-synuclein to medical instruments and subsequent exposure of patients to α-synuclein similar to what has been observed in iatrogenic transmission of prions. Here, we evaluated adsorption and desorption of α-synuclein to two surfaces: stainless steel and a gold surface coated with a 11-Amino-1-undecanethiol hydrochloride self-assembled-monolayer (SAM) using in-situ combinatorial quartz crystal microbalance with dissipation and spectroscopic ellipsometry. α-Synuclein was found to attach to both surfaces, however, increased α-synuclein adsorption was observed onto the positively charged SAM surface compared to the stainless steel surface. Dynamic light scattering data showed that larger α-synuclein fibrils were preferentially attached to the stainless steel surface when compared with the distributions in the original α-synuclein solution and on the SAM surface. We determined that after attachment, introduction of a 1N NaOH solution could completely remove α-synuclein adsorbed on the stainless steel surface while α-synuclein was retained on the SAM surface. Our results indicate α-synuclein can bind to multiple surface types and that decontamination is surface-dependent.

Human α-Synuclein Inhibits Platelets Aggregation in vitro by Interfering with the α-Thrombin/Protease-Activated Receptor 1 Functional Axis

“…This might in principle hinder binding of platelets to the electrode surface, thus reducing stimulated platelets aggregation in MEA measurements, compared to controls, with a resulting apparent (artefactual) higher antiaggregating effect of αSyn. However, this possibility can be safely ruled out considering that: i) αSyn binds to metal surfaces in the fibrillar state, not in the monomeric state (37); ii) the lag phase of αSyn fibril formation, even in a crowded environment, is much longer (~3 h) than the time scale of MEA analysis (i.e. 6-10 min) (11); iii) finally, the tendency of αSyn oligomers/polymers to stick on metal surfaces is 2-3 times lower than that measured for albumin (37), which is even much more concentrated in the blood (260-380 μM) than the maximal αSyn concentration explored in this study (20 μM).…”

“…Notably, Syn has been reported to interact with metal surfaces (e.g. stainless steel and gold) (37). This might in principle hinder binding of platelets to the electrode surface, thus reducing stimulated platelets aggregation in MEA measurements, compared to controls, with a resulting apparent (artefactual) higher antiaggregating effect of Syn.…”

Corrosion Behavior and In Vitro Cytotoxicity of Ni–Ti and Stainless Steel Arch Wires Exposed to Lysozyme, Ovalbumin, and Bovine Serum Albumin

“…Therefore, the effects of protein on the corrosion process of alloys may be due to the amino acid sequence, spatial conformation, conformational stability, or flexibility under changing ionic conditions. 47 , 48 These factors illustrate the complexity in the process of protein interactions with alloy.…”

Spin-Dependent Ionization of Chiral Molecular Films

“…48,49 Thus, positively charged SAMs of achiral 11-amino-1-undecanethiolate (AUT) monolayers were formed first on FM substrates ( Figure S12) to facilitate the electrostatic binding of BSA molecules by association with negatively charged residues on the proteins. 50 In its native conformation, the globular protein, BSA, is composed of multiple right-handed α-helical subunits with ca. 60% structural helicity.…”