Evidence map›Paper›PMID 26707645›Full record

ArticleBiochemical and biophysical research communications2016

A hyperbranched dopamine-containing PEG-based polymer for the inhibition of α-synuclein fibrillation.

Leonid Breydo, Ben Newland, Hong Zhang, Anne Rosser, Carsten Werner, Vladimir N Uversky, Wenxin Wang

Open access · hybridAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

7 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Mitigation of Amyloidosis with Nanomaterials.Advanced materials (Deerfield Beach, Fla.) · 2020
    Review
  6. A health concern regarding the protein corona, aggregation and disaggregation.Biochimica et biophysica acta. General subjects · 2019
    Review
  7. 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

7 authors at 5 institutions in 7 countries.

Leonid BreydoDepartment of Molecular Medicine and Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, 33612 Tampa, FL, USA. Electronic address: lbreydo@health.usf.edu.
Ben NewlandLeibniz-Institute für Polymerforschung, Dresden, Germany; Brain Repair Group, School of Biosciences, Cardiff University, Cardiff, UK.
Hong ZhangThe Charles Institute of Dermatology, School of Medicine and Medical Science, University College Dublin, Dublin, Ireland.
Anne RosserBrain Repair Group, School of Biosciences, Cardiff University, Cardiff, UK.
Carsten WernerLeibniz-Institute für Polymerforschung, Dresden, Germany.
Vladimir N UverskyDepartment of Molecular Medicine and Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, 33612 Tampa, FL, USA; Institute for Biological Instrumentation, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia; Department of Biological Sciences, Faculty of Science, King Abdulaziz University, PO Box 80203, 21589 Jeddah, Saudi Arabia.
Wenxin WangThe Charles Institute of Dermatology, School of Medicine and Medical Science, University College Dublin, Dublin, Ireland; School of Materials Science and Engineering, Tianjin University, Tianjin, China.
Leibniz Institute of Polymer Research · DEUniversity of South Florida · USCardiff University · GBTianjin University · CNUniversity College Dublin · IE

Funding

Medical Research Council MR/L010305/1Wellcome Trust
6 · The paper itself

Abstract

Aggregation of α-synuclein is believed to play an important role in Parkinson's disease and in other neurodegenerative maladies. Small molecule inhibitors of this process are among the most promising drug candidates for neurodegenerative diseases. Dendrimers have also been studied for anti-fibrillation applications but they can be difficult and expensive to synthetize. Here we show that RAFT polymerization can be used to produce a hyperbranched polyethylene glycol structure via a one-pot reaction. This polymer included a dopamine moiety, a known inhibitor of α-synuclein fibril formation. Dopamine within the polymer structure was capable of aggregation inhibition, although not to the same degree as free dopamine. This result opens up new avenues for the use of controlled radical polymerizations as a means of preparing hyperbranched polymers for anti-fibrillation activity, but shows that the incorporation of functional groups from known small molecules within polymers may alter their biological activity.

Indexed as

alpha-SynucleinAmyloidDimerizationDopamineDrug CompoundingPolyethylene GlycolsProtein Bindingalpha-SynucleinAmyloidDopaminePolyethylene GlycolsDopamineHyperbranched polymersMacromolecular crowdingParkinson's diseaseProtein aggregationRAFT polymerizationα-synuclein

Identifiers

PMID26707645
PMCPMC4727786
OpenAlexW2210448351

What OpenQuestion holds

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LicenceCC BY
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.