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

作者: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*
来源:Colloids and Surfaces B: Biointerfaces , 2018, 166: 98-107.
DOI:10.1016/j.colsurfb.2018.03.011

摘要

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

  • 出版日期2018-6-1