Evidence map›Paper›PMID 19260715›Full record

ArticleThe journal of physical chemistry. B2009

A kinetic model for beta-amyloid adsorption at the air/solution interface and its implication to the beta-amyloid aggregation process.

Dianlu Jiang, Kim Lien Dinh, Travis C Ruthenburg, Yi Zhang, Lei Su, Donald P Land, Feimeng Zhou

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2009. 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
2.5field-weighted citation impact, top 12% 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, 51 citations in OpenAlex.

  1. Article
  2. Adsorption free energy predicts amyloid protein nucleation rates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Article
  4. Article
  5. Review
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  7. The Journal of biological chemistry · 2019
    Article
  8. Effect of FeScanning · 2019
    Article
  9. Interfacial Properties of NBiophysical journal · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
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  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

7 authors at 2 institutions in 1 country.

Dianlu JiangDepartment of Chemistry and Biochemistry, California State University, Los Angeles, Los Angeles, California 90032, USA.
Kim Lien Dinh
Travis C Ruthenburg
Yi Zhang
Lei Su
Donald P Land
Feimeng Zhou
California State University Los Angeles · USUniversity of California, Davis · US

Funding

Voltammetric, Surface, and Kinetic Studies of p53 and Amyloidogenic ProteinsS06GM008101 · NIGMS · CALIFORNIA STATE UNIVERSITY LOS ANGELES · PI GUTIERREZ, CARLOS GABRIEL · 1989 to 2008
$20.8M
NOVEL DRUG DESIGN AND HIGH THROUGHPUT SCREENINGP20MD001824 · NIMHD · CALIFORNIA STATE UNIVERSITY LOS ANGELES · PI MODARRES, ALI · 2005 to 2009
$4.4M
NIGMS NIH HHS GM 08101NIGMS NIH HHS S06 GM008101NIMHD NIH HHS P20 MD001824
6 · The paper itself

Abstract

At the air/buffer solution interface the kinetics of adsorption of amyloid beta peptide, Abeta(1-42), whose bulk concentration (submicromolar) is more than 2 orders of magnitude lower than that typically used in other in vitro aggregation studies, has been studied using a Langmuir-Blodgett trough. The pressure-time curves exhibit a lag phase, wherein the surface pressure essentially remains at zero, and a rising phase, corresponding to the Abeta adsorption at the interface. The duration of the lag phase was found to be highly dependent on both the Abeta bulk concentration and the solution temperature. A large activation energy (62.2 +/- 4.1 KJ/mol) was determined and the apparent adsorption rate constant was found to be linearly dependent on the Abeta bulk concentration. Attenuated total reflection-IR spectra of the adsorbed Abeta transferred to a solid substrate and circular dichroism measurements of Abeta in the solution layer near the interface reveal that the natively unstructured Abeta in the bulk undergo a conformation change (folding) to mainly the alpha-helical structure. The results suggest that, prior to the adsorption step, an equilibrium between Abeta conformations is established within the subsurface. The kinetic equation derived from this model confirms that the overall Abeta adsorption is kinetically controlled and the apparent rate constant is proportional to the Abeta bulk concentration. This model also indicates that interfaces such as cell membranes and lipid bilayers may facilitate Abeta aggregation/ fibrillation by providing a thin hydrophobic layer adjacent to the interface for the initial A/beta conformation change (misfolding) and accumulation. Such a preconcentration effect offers a plausible explanation of the fact that Abeta fibrillation occurs in vivo at nanomolar concentrations. Another important biological implication from our work is that Abeta misfolding may occur before its adsorption onto a cell membrane. This general kinetic model should also find applications in adsorption studies of other types of biomolecules whose overall kinetics exhibits a lag phase that is dependent on the bulk concentration of the adsorbate.

Indexed as

AdsorptionAirAmyloid beta-PeptidesBiophysicsChemistry, PhysicalCircular DichroismHumansKineticsMicroscopy, Atomic ForcePeptidesProtein BindingSolutionsSpectroscopy, Fourier Transform InfraredSurface PropertiesWaterAmyloid beta-PeptidesPeptidesSolutionsWater

Identifiers

PMID19260715
PMCPMC3222685
OpenAlexW1993389565

What OpenQuestion holds

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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.