Evidence map›Paper›PMID 30250131›Full record

ArticleNature communications2018

Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity.

Francesco Simone Ruggeri, Jerome Charmet, Tadas Kartanas, Quentin Peter, Sean Chia, Johnny Habchi, Christopher M Dobson, Michele Vendruscolo, Tuomas P J Knowles

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

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  18. Lipids uniquely alter rates of insulin aggregation and lower toxicity of amyloid aggregates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2023
    Article
  19. Review
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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.

Francesco Simone RuggeriDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Jerome CharmetDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0001-6992-4090
Tadas KartanasDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Quentin PeterDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0002-8018-3059
Sean ChiaDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Johnny HabchiDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Michele VendruscoloDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0002-3616-1610
Tuomas P J KnowlesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK. tpjk2@cam.ac.uk.

Funding

European Research Council 337969
6 · The paper itself

Abstract

Scanning probe microscopy provides a unique window into the morphology, mechanics, and structure of proteins and their complexes on the nanoscale. Such measurements require, however, deposition of samples onto substrates. This process can affect conformations and assembly states of the molecular species under investigation and can bias the molecular populations observed in heterogeneous samples through differential adsorption. Here, we show that these limitations can be overcome with a single-step microfluidic spray deposition platform. This method transfers biological solutions to substrates as microdroplets with subpicoliter volume, drying in milliseconds, a timescale that is shorter than typical diffusion times of proteins on liquid-solid interfaces, thus avoiding surface mass transport and change to the assembly state. Finally, the single-step deposition ensures the attachment of the full molecular content of the sample to the substrate, allowing quantitative measurements of different molecular populations within heterogeneous systems, including protein aggregates.

Indexed as

alpha-SynucleinAmyloid beta-PeptidesAnalytic Sample Preparation MethodsFeasibility StudiesMicrofluidicsMicroscopy, Atomic ForcePeptide FragmentsProtein AggregatesSingle Molecule Imagingalpha-SynucleinAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Peptide FragmentsProtein AggregatesSNCA protein, human

Identifiers

PMID30250131
PMCPMC6155325

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Registered trials

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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.