Evidence map›Paper›PMID 29284092›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2018

Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces.

Giulio Tesei, Erik Hellstrand, Kalyani Sanagavarapu, Sara Linse, Emma Sparr, Robert Vácha, Mikael Lund

Open access · greenAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 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
0.3field-weighted citation impact, top 39% 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, 5 citations in OpenAlex.

  1. Time-Resolved In Situ AFM Measurement of Growth Rates of Aβ40 Fibrils.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  2. Frustrated peptide chains at the fibril tip control the kinetics of growth of amyloid-β fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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 1 institution in 2 countries.

Giulio TeseiTheoretical Chemistry, ‡Biophysical Chemistry, §Biochemistry & Structural Biology, and ∥Physical Chemistry, Lund University , 221 00 Lund, Sweden.ORCID 0000-0003-4339-4460
Erik HellstrandTheoretical Chemistry, ‡Biophysical Chemistry, §Biochemistry & Structural Biology, and ∥Physical Chemistry, Lund University , 221 00 Lund, Sweden.
Kalyani SanagavarapuTheoretical Chemistry, ‡Biophysical Chemistry, §Biochemistry & Structural Biology, and ∥Physical Chemistry, Lund University , 221 00 Lund, Sweden.
Sara LinseTheoretical Chemistry, ‡Biophysical Chemistry, §Biochemistry & Structural Biology, and ∥Physical Chemistry, Lund University , 221 00 Lund, Sweden.
Emma SparrTheoretical Chemistry, ‡Biophysical Chemistry, §Biochemistry & Structural Biology, and ∥Physical Chemistry, Lund University , 221 00 Lund, Sweden.
Robert VáchaTheoretical Chemistry, ‡Biophysical Chemistry, §Biochemistry & Structural Biology, and ∥Physical Chemistry, Lund University , 221 00 Lund, Sweden.
Mikael LundTheoretical Chemistry, ‡Biophysical Chemistry, §Biochemistry & Structural Biology, and ∥Physical Chemistry, Lund University , 221 00 Lund, Sweden.
Central European Institute of Technology · CZ

Funding

European Research Council 340890
6 · The paper itself

Abstract

Amyloid aggregates are associated with a range of human neurodegenerative disorders, and it has been shown that neurotoxicity is dependent on aggregate size. Combining molecular simulation with analytical theory, a predictive model is proposed for the adsorption of amyloid aggregates onto oppositely charged surfaces, where the interaction is governed by an interplay between electrostatic attraction and entropic repulsion. Predictions are experimentally validated against quartz crystal microbalance-dissipation experiments of amyloid beta peptides and fragmented fibrils in the presence of a supported lipid bilayer. Assuming amyloids as rigid, elongated particles, we observe nonmonotonic trends for the extent of adsorption with respect to aggregate size and preferential adsorption of smaller aggregates over larger ones. Our findings describe a general phenomenon with implications for stiff polyions and rodlike particles that are electrostatically attracted to a surface.

Indexed as

AdsorptionAmyloidAmyloid beta-PeptidesQuartz Crystal Microbalance TechniquesSurface PropertiesAmyloidAmyloid beta-Peptides

Identifiers

PMID29284092
PMCPMC5828364
OpenAlexW2776830312

What OpenQuestion holds

Textmetadata
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.