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Adsorption and decontamination of ?-synuclein from medically and environmentally-relevant surfaces.


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

SUBMITTER: Phan HTM 

PROVIDER: S-EPMC5911191 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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

Phan Hanh T M HTM   Bartz Jason C JC   Ayers Jacob J   Giasson Benoit I BI   Schubert Mathias M   Rodenhausen Keith B KB   Kananizadeh Negin N   Li Yusong Y   Bartelt-Hunt Shannon L SL  

Colloids and surfaces. B, Biointerfaces 20180309


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 wh  ...[more]

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