Evidence map›Paper›PMID 18510376›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2008

Double cushions preserve transmembrane protein mobility in supported bilayer systems.

Arnaldo J Diaz, Fernando Albertorio, Susan Daniel, Paul S Cremer

Abstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2008. 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
3.9field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. Lipid-Substrate Interactions Lead to Bilayer Asymmetry.Journal of the American Chemical Society · 2026
    Article
  3. Article
  4. Article
  5. Binding ofLangmuir : the ACS journal of surfaces and colloids · 2024
    Article
  6. Article
  7. Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Supported lipid bilayer platforms to probe cell mechanobiology.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  14. Article
  15. Article
  16. Electronic control of HNature communications · 2016
    Article
  17. Article
  18. Article
  19. Article
  20. 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.

Arnaldo J DiazDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Fernando Albertorio
Susan Daniel
Paul S Cremer
Texas A&M University · US

Funding

Multivalent Ligand-Receptor Binding on Lipid BilayersR01GM070622 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI CREMER, PAUL · 2004 to 2012
$2.2M
Protein Supported Lipid Bilayers as a Mimic of Native Biological MembranesF31GM072434 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI DIAZ, ARNALDO J · 2005 to 2007
$82k
NIGMS NIH HHS 5 F31 GM072434-03NIGMS NIH HHS F31 GM072434NIGMS NIH HHS R01 GM070622PHS HHS R01-070622
6 · The paper itself

Abstract

Supported lipid bilayers (SLBs) have been widely used as model systems to study cell membrane processes because they preserve the same 2D membrane fluidity found in living cells. One of the most significant limitations of this platform, however, is its inability to incorporate mobile transmembrane species. It is often postulated that transmembrane proteins reconstituted in SLBs lose their mobility because of direct interactions between the protein and the underlying substrate. Herein, we demonstrate a highly mobile fraction for a transmembrane protein, annexin V. Our strategy involves supporting the lipid bilayer on a double cushion, where we not only create a large space to accommodate the transmembrane portion of the macromolecule but also passivate the underlying substrate to reduce nonspecific protein-substrate interactions. The thickness of the confined water layer can be tuned by fusing vesicles containing polyethyleneglycol (PEG)-conjugated lipids of various molecular weights to a glass substrate that has first been passivated with a sacrificial layer of bovine serum albumin (BSA). The 2D fluidity of these systems was characterized by fluorescence recovery after photobleaching (FRAP) measurements. Uniform, mobile phospholipid bilayers with lipid diffusion coefficients of around 3 x 10(-8) cm2/s and percent mobile fractions of over 95% were obtained. Moreover, we obtained annexin V diffusion coefficients that were also around 3 x 10(-8) cm2/s with mobile fractions of up to 75%. This represents a significant improvement over bilayer platforms fabricated directly on glass or using single cushion strategies.

Indexed as

AnimalsAnnexin A5CattleCell MembraneDiffusionLipid BilayersPolymersSerum Albumin, BovineAnnexin A5Lipid BilayersPolymersSerum Albumin, Bovine

Identifiers

PMID18510376
PMCPMC3475160
OpenAlexW1964196663

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.