Evidence map›Paper›PMID 19527662›Full record

ArticleBiophysical journal2009

Self-assembly of phenylalanine oligopeptides: insights from experiments and simulations.

Phanourios Tamamis, Lihi Adler-Abramovich, Meital Reches, Karen Marshall, Pawel Sikorski, Louise Serpell, Ehud Gazit, Georgios Archontis

Abstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing 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

65 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Protopeptide backbone affects assembly in aqueous solutions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Review
  11. Self-Assembly Properties of Xylene-Derived Constitutional Isomers of Fmoc-Phenylalanine.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Peptide Self-Assembled Nanocarriers for Cancer Drug Delivery.The journal of physical chemistry. B · 2023
    Review
  18. Short Peptide-Based Smart Thixotropic Hydrogels.Gels (Basel, Switzerland) · 2022
    Review
  19. Article
  20. Article

5 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

8 authors.

Phanourios TamamisDepartment of Physics, University of Cyprus, Nicosia, Cyprus.
Lihi Adler-Abramovich
Meital Reches
Karen Marshall
Pawel Sikorski
Louise Serpell
Ehud Gazit
Georgios Archontis

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Studies of peptide-based nanostructures provide general insights into biomolecular self-assembly and can lead material engineering toward technological applications. The diphenylalanine peptide (FF) self-assembles into discrete, hollow, well ordered nanotubes, and its derivatives form nanoassemblies of various morphologies. Here we demonstrate for the first time, to our knowledge, the formation of planar nanostructures with beta-sheet content by the triphenylalanine peptide (FFF). We characterize these structures using various microscopy and spectroscopy techniques. We also obtain insights into the interactions and structural properties of the FF and FFF nanostructures by 0.4-micros, implicit-solvent, replica-exchange, molecular-dynamics simulations of aqueous FF and FFF solutions. In the simulations the peptides form aggregates, which often contain open or ring-like peptide networks, as well as elementary and network-containing structures with beta-sheet characteristics. The networks are stabilized by polar and nonpolar interactions, and by the surrounding aggregate. In particular, the charged termini of neighbor peptides are involved in hydrogen-bonding interactions and their aromatic side chains form "T-shaped" contacts, as in three-dimensional FF crystals. These interactions may assist the FF and FFF self-assembly at the early stage, and may also stabilize the mature nanostructures. The FFF peptides have higher network propensities and increased aggregate stabilities with respect to FF, which can be interpreted energetically.

Indexed as

Computer SimulationHydrogen BondingMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionModels, MolecularNanostructuresOligopeptidesPhenylalanineProtein Structure, SecondaryProtein Structure, TertiarySolutionsOligopeptidesPhenylalanineSolutions

Identifiers

PMID19527662
PMCPMC2712050

What OpenQuestion holds

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Registered trials

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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.