Evidence map›Paper›PMID 28558246›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2017

Buffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks.

Nicholas A Kurniawan, Thomas H S van Kempen, Stijn Sonneveld, Tilaï T Rosalina, Bart E Vos, Karin A Jansen, Gerrit W M Peters, Frans N van de Vosse, Gijsje H Koenderink

Open access · hybridAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Depletion-Induced Self-Assembly of Colloidal Particles on a Solid Substrate.Langmuir : the ACS journal of surfaces and colloids · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Fibrin-based Bioinks: New Tricks from an Old Dog.International journal of bioprinting · 2020
    Review
  18. 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 2 countries.

Nicholas A KurniawanDepartment of Systems Biophysics, AMOLF , Amsterdam 1009 DB, The Netherlands.
Thomas H S van Kempen
Stijn SonneveldDepartment of Systems Biophysics, AMOLF , Amsterdam 1009 DB, The Netherlands.
Tilaï T Rosalina
Bart E VosDepartment of Systems Biophysics, AMOLF , Amsterdam 1009 DB, The Netherlands.
Karin A JansenDepartment of Systems Biophysics, AMOLF , Amsterdam 1009 DB, The Netherlands.
Gerrit W M PetersORCID 0000-0001-7208-5128
Frans N van de Vosse
Gijsje H KoenderinkDepartment of Systems Biophysics, AMOLF , Amsterdam 1009 DB, The Netherlands.ORCID 0000-0002-7823-8807
Institute for Atomic and Molecular Physics · NLInstitute for Complex Systems · ITEindhoven University of Technology · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibrin is a plasma protein with a central role in blood clotting and wound repair. Upon vascular injury, fibrin forms resilient fibrillar networks (clots) via a multistep self-assembly process, from monomers, to double-stranded protofibrils, to a branched network of thick fibers. In vitro, fibrin self-assembly is sensitive to physicochemical conditions like the solution pH and ionic strength, which tune the strength of the noncovalent driving forces. Here we report a surprising finding that the buffer-which is necessary to control the pH and is typically considered to be inert-also significantly influences fibrin self-assembly. We show by confocal microscopy and quantitative light scattering that various common buffering agents have no effect on the initial assembly of fibrin monomers into protofibrils but strongly hamper the subsequent lateral association of protofibrils into thicker fibers. We further find that the structural changes are independent of the molecular structure of the buffering agents as well as of the activation mechanism and even occur in fibrin networks formed from platelet-poor plasma. This buffer-mediated decrease in protofibril bundling results in a marked reduction in the permeability of fibrin networks but only weakly influences the elastic modulus of fibrin networks, providing a useful tuning parameter to independently control the elastic properties and the permeability of fibrin networks. Our work raises the possibility that fibrin assembly in vivo may be regulated by variations in the acute-phase levels of bicarbonate and phosphate, which act as physiological buffering agents of blood pH. Moreover, our findings add a new example of buffer-induced effects on biomolecular self-assembly to recent findings for a range of proteins and lipids.

Indexed as

Blood CoagulationBuffersFibrinFibrinogenMacromolecular SubstancesBuffersFibrinFibrinogenMacromolecular Substances

Identifiers

PMID28558246
PMCPMC5489959
OpenAlexW2617620306

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.