Evidence map›Paper›PMID 12930900›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Biomimetic organization: Octapeptide self-assembly into nanotubes of viral capsid-like dimension.

Céline Valéry, Maïté Paternostre, Bruno Robert, Thaddée Gulik-Krzywicki, Theyencheri Narayanan, Jean-Claude Dedieu, Gérard Keller, Maria-Luisa Torres, Roland Cherif-Cheikh, Pilar Calvo and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed, 1 pooled it
4.5field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 1 synthesis or guideline pooled it, 271 citations in OpenAlex.

  1. Pooled it
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  12. Article
  13. Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Polymorphism in peptide self-assembly visualized.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Atomic structure of Lanreotide nanotubes revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Self-Assembling Peptides: From Design to Biomedical Applications.International journal of molecular sciences · 2021
    Review
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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

11 authors at 1 institution in 1 country.

Céline ValéryUnité Mixte de Recherche 8612, Centre National de la Recherche Scientifique, Faculté de Pharmacie, 5 Rue J.B. Clément, 92296 Châtenay-Malabry Cedex, France.
Maïté Paternostre
Bruno Robert
Thaddée Gulik-Krzywicki
Theyencheri Narayanan
Jean-Claude Dedieu
Gérard Keller
Maria-Luisa Torres
Roland Cherif-Cheikh
Pilar Calvo
Franck Artzner
Commissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The controlled self-assembly of complex molecules into well defined hierarchical structures is a promising route for fabricating nanostructures. These nanoscale structures can be realized by naturally occurring proteins such as tobacco mosaic virus, capsid proteins, tubulin, actin, etc. Here, we report a simple alternative method based on self-assembling nanotubes formed by a synthetic therapeutic octapeptide, Lanreotide in water. We used a multidisciplinary approach involving optical and electron microscopies, vibrational spectroscopies, and small and wide angle x-ray scattering to elucidate the hierarchy of structures exhibited by this system. The results revealed the hexagonal packing of nanotubes, and high degree of monodispersity in the tube diameter (244 A) and wall thickness (approximately equal to 18 A). Moreover, the diameter is tunable by suitable modifications in the molecular structure. The self-assembly of the nanotubes occurs through the association of beta-sheets driven by amphiphilicity and a systematic aromatic/aliphatic side chain segregation. This original and simple system is a unique example for the study of complex self-assembling processes generated by de novo molecules or amyloid peptides.

Indexed as

BiomimeticsCapsidModels, MolecularPeptides, CyclicProtein ConformationProtein Structure, SecondarySomatostatinlanreotidePeptides, CyclicSomatostatin

Identifiers

PMID12930900
PMCPMC193548
OpenAlexW2162909533

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.