Evidence map›Paper›PMID 21391676›Full record

ArticleJournal of the American Chemical Society2011

Single-molecule resolution of interfacial fibrinogen behavior: effects of oligomer populations and surface chemistry.

Mark Kastantin, Blake B Langdon, Erin L Chang, Daniel K Schwartz

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

16 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Single-molecule resolution of protein structure and interfacial dynamics on biomaterial surfaces.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. DNA hairpin stabilization on a hydrophobic surface.Small (Weinheim an der Bergstrasse, Germany) · 2013
    Article
  12. Article
  13. Identifying mechanisms of interfacial dynamics using single-molecule tracking.Langmuir : the ACS journal of surfaces and colloids · 2012
    Review
  14. Distinguishing positional uncertainty from true mobility in single-molecule trajectories that exhibit multiple diffusive modes.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2012
    Article
  15. Article
  16. 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

4 authors at 1 institution in 1 country.

Mark KastantinDepartment of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, USA.
Blake B Langdon
Erin L Chang
Daniel K Schwartz
University of Colorado Boulder · US

Funding

Behavior of biomolecules at controllable solid - water interfacesF32GM091777 · NIGMS · UNIVERSITY OF COLORADO · PI KASTANTIN, MARK JOSEPH · 2010 to 2011
$94k
NIGMS NIH HHS 1F32GM091777-01NIGMS NIH HHS F32 GM091777NIGMS NIH HHS F32 GM091777-01
6 · The paper itself

Abstract

Through the use of single-molecule total internal reflection fluorescence microscopy, the dynamic behavior of fibrinogen was observed at the interface between aqueous solution and various solid surfaces. Multiple populations of objects were observed, as characterized by surface residence times, interfacial diffusion, and fluorescence intensity. On all surfaces, populations exhibited direct links between surface residence time, rate of diffusion, and fluorescence intensity. In particular, longer-lived populations diffused more slowly and exhibited greater fluorescence intensity, leading to the conclusion that the objects represented fibrinogen monomers and discrete oligomer populations (dimers, trimers, etc.), and that these oligomer populations play an important role in the protein-surface interaction because of their long surface residence times. Two or three diffusive modes were observed for most populations, indicating that protein aggregates have multiple mechanisms for interaction with solid substrates. In addition, the fastest diffusive mode is believed to represent a hopping mode that often precedes desorption events. Surprisingly, a monolayer of 5000 Da poly(ethylene glycol) (PEG5000) increased surface residence time and slowed diffusion of fibrinogen relative to bare fused silica or hydrophobically modified fused silica, suggesting that the mechanism of PEG resistance to protein adhesion is more sophisticated than the simple repulsion of individual proteins.

Indexed as

AdsorptionFibrinogenHumansHydrophobic and Hydrophilic InteractionsMicroscopy, FluorescencePolyethylene GlycolsSilicon DioxideSolutionsSurface PropertiesWaterFibrinogenPolyethylene GlycolsSilicon DioxideSolutionsWater

Identifiers

PMID21391676
PMCPMC3077424
OpenAlexW2047695034

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.