Evidence map›Paper›PMID 17535898›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Docosahexaenoic acid alters bilayer elastic properties.

Michael J Bruno, Roger E Koeppe, Olaf S Andersen

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
3.8field-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

90 citing papers in PubMed, 149 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Impact of Elovl5 Deficiency on Cerebellar Excitatory Synaptic Transmission in Mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
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  7. Review
  8. Article
  9. Article
  10. Do patients benefit from omega-3 fatty acids?Cardiovascular research · 2024
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

30 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Michael J BrunoDepartment of Physiology and Biophysics, Weill Medical College of Cornell University, New York, NY 10021, USA.
Roger E Koeppe
Olaf S Andersen
Cornell University · USUniversity of Arkansas at Fayetteville · US

Funding

Structure based drug discoveryP20RR015569 · NCRR · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2000 to 2009
$21.4M
Energetics of Channel-Bilayer InteractionsR01GM021342 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI ANDERSEN, OLAF S. · 1985 to 2021
$9.9M
NCRR NIH HHS P20 RR015569NCRR NIH HHS RR15569NIGMS NIH HHS GM021342NIGMS NIH HHS R01 GM021342
6 · The paper itself

Abstract

At low micromolar concentrations, polyunsaturated fatty acids (PUFAs) alter the function of many membrane proteins. PUFAs exert their effects on unrelated proteins at similar concentrations, suggesting a common mode of action. Because lipid bilayers serve as the common "solvent" for membrane proteins, the common mechanism could be that PUFAs adsorb to the bilayer/solution interface to promote a negative-going change in lipid intrinsic curvature and, like other reversibly adsorbing amphiphiles, increase bilayer elasticity. PUFA adsorption thus would alter the bilayer deformation energy associated with protein conformational changes involving the protein/bilayer boundary, which would alter protein function. To explore the feasibility of such a mechanism, we used gramicidin (gA) analogues of different lengths together with bilayers of different thicknesses to assess whether docosahexaenoic acid (DHA) could exert its effects through a bilayer-mediated mechanism. Indeed, DHA increases gA channel appearance rates and lifetimes and decreases the free energy of channel formation. The appearance rate and lifetime changes increase with increasing channel-bilayer hydrophobic mismatch and are not related to differing DHA bilayer absorption coefficients. DHA thus alters bilayer elastic properties, not just lipid intrinsic curvature; the elasticity changes are important for DHA's bilayer-modifying actions. Oleic acid (OA), which has little effect on membrane protein function, exerts no such effects despite OA's adsorption coefficient being an order of magnitude greater than DHA's. These results suggest that DHA (and other PUFAs) may modulate membrane protein function by bilayer-mediated mechanisms that do not involve specific protein binding but rather changes in bilayer material properties.

Indexed as

AbsorptionDocosahexaenoic AcidsElasticityGramicidinLipid BilayersMembrane ProteinsDocosahexaenoic AcidsGramicidinLipid BilayersMembrane Proteins

Identifiers

PMID17535898
PMCPMC1887599
OpenAlexW2124138679

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.