PubAg

Main content area

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

Author:
Phan, Hanh T.M., Bartz, Jason C., Ayers, Jacob, Giasson, Benoit I., Schubert, Mathias, Rodenhausen, Keith B., Kananizadeh, Negin, Li, Yusong, Bartelt-Hunt, Shannon L.
Source:
Colloids and surfaces 2018 v.166 pp. 98-107
ISSN:
0927-7765
Subject:
Parkinson disease, adsorption, atrophy, colloids, decontamination, desorption, gold, light scattering, medical equipment, patients, prion diseases, prions, quartz crystal microbalance, sodium hydroxide, spectroscopy, stainless steel
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.
Agid:
5919122