Evidence map›Paper›PMID 29550546›Full record

ArticleColloids and surfaces. B, Biointerfaces2018

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

Hanh T M Phan, Jason C Bartz, Jacob Ayers, Benoit I Giasson, Mathias Schubert, Keith B Rodenhausen, Negin Kananizadeh, Yusong Li, Shannon L Bartelt-Hunt

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Colloids and surfaces. B, Biointerfaces, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Hanh T M PhanDepartment of Civil Engineering, University of Nebraska-Lincoln, United States; Center for Nanohybrid Functional Materials, University of Nebraska-Lincoln, United States.
Jason C BartzDepartment of Medical Microbiology and Immunology, Creighton University, United States.
Jacob AyersDepartment of Neuroscience, University of Florida, United States.
Benoit I GiassonDepartment of Neuroscience, University of Florida, United States.
Mathias SchubertDepartment of Electrical and Computer Engineering, University of Nebraska-Lincoln, United States; Center for Nanohybrid Functional Materials, University of Nebraska-Lincoln, United States.
Keith B RodenhausenDepartment of Electrical and Computer Engineering, University of Nebraska-Lincoln, United States; Center for Nanohybrid Functional Materials, University of Nebraska-Lincoln, United States; Biolin Scientific, Inc., Paramus, NJ, United States.
Negin KananizadehDepartment of Civil Engineering, University of Nebraska-Lincoln, United States; Center for Nanohybrid Functional Materials, University of Nebraska-Lincoln, United States.
Yusong LiDepartment of Civil Engineering, University of Nebraska-Lincoln, United States.
Shannon L Bartelt-HuntDepartment of Civil Engineering, University of Nebraska-Lincoln, United States; Center for Nanohybrid Functional Materials, University of Nebraska-Lincoln, United States. Electronic address: sbartelt2@unl.edu.
University of Nebraska–Lincoln · USUniversity of Florida · USCreighton University · US

Funding

Mechanisms of Aggregated Alpha-Synuclein Induction and ProgressionR01NS089622 · NINDS · UNIVERSITY OF FLORIDA · PI GIASSON, BENOIT I · 2014 to 2018
$1.6M
NINDS NIH HHS R01 NS089622
6 · The paper itself

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.

Indexed as

alpha-SynucleinProtein ConformationStainless SteelSurface Propertiesalpha-SynucleinStainless SteelAdsorptionDecontaminationProtein conformationProtein orientationQCM-DSpectroscopic ellipsometryStainless steelα-Synuclein

Identifiers

PMID29550546
PMCPMC5911191
OpenAlexW2793747695

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.