Evidence map›Paper›PMID 22500762›Full record

ArticleBiophysical journal2012

End-to-end self-assembly of RADA 16-I nanofibrils in aqueous solutions.

Paolo Arosio, Marta Owczarz, Hua Wu, Alessandro Butté, Massimo Morbidelli

Abstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. First Safety and Performance Evaluation of T45K, a Self-Assembling Peptide Barrier Hemostatic Device, After Skin Lesion Excision.Dermatologic surgery : official publication for American Society for Dermatologic Surgery [et al.] · 2018
    Trial
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Polymeric Hydrogels for In Vitro 3D Ovarian Cancer Modeling.International journal of molecular sciences · 2022
    Review
  11. Self-Assembling Peptides: From Design to Biomedical Applications.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. On the lag phase in amyloid fibril formation.Physical chemistry chemical physics : PCCP · 2015
    Review
  17. 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

5 authors.

Paolo ArosioInstitute for Chemical and Bioengineering, Department of Chemistry and Applied Biosciences, Zurich, Switzerland.
Marta Owczarz
Hua Wu
Alessandro Butté
Massimo Morbidelli

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RADARADARADARADA (RADA 16-I) is a synthetic amphiphilic peptide designed to self-assemble in a controlled way into fibrils and higher ordered structures depending on pH. In this work, we use various techniques to investigate the state of the peptide dispersed in water under dilute conditions at different pH and in the presence of trifluoroacetic acid or hydrochloric acid. We have identified stable RADA 16-I fibrils at pH 2.0-4.5, which have a length of ∼200-400 nm and diameter of 10 nm. The fibrils have the characteristic antiparallel β-sheet structure of amyloid fibrils, as measured by circular dichroism and Fourier transform infrared spectrometry. During incubation at pH 2.0-4.5, the fibrils elongate very slowly via an end-to-end fibril-fibril aggregation mechanism, without changing their diameter, and the kinetics of such aggregation depends on pH and anion type. At pH 2.0, we also observed a substantial amount of monomers in the system, which do not participate in the fibril elongation and degrade to fragments. The fibril-fibril elongation kinetics has been simulated using the Smoluchowski kinetic model, population balance equations, and the simulation results are in good agreement with the experimental data. It is also found that the aggregation process is not limited by diffusion but rather is an activated process with energy barrier in the order of 20 kcal/mol.

Indexed as

Protein MultimerizationAmino Acid SequenceHydrogen-Ion ConcentrationKineticsMolecular Sequence DataNanostructuresPeptidesProtein StabilitySolutionsTemperatureWaterPeptidesSolutionsWater

Identifiers

PMID22500762
PMCPMC3318125

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.