Evidence map›Paper›PMID 36509953›Full record

ArticleAdvanced materials (Deerfield Beach, Fla.)2023

Understanding Self-Assembly of Silica-Precipitating Peptides to Control Silica Particle Morphology.

Johannes Strobl, Fanny Kozak, Meder Kamalov, Daniela Reichinger, Dennis Kurzbach, Christian Fw Becker

Abstract read
In one paragraph

Article in Advanced materials (Deerfield Beach, Fla.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. The structure of His15 acetamide-modified hen egg-white lysozyme: a nice surprise from an old friend.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  5. Review
  6. Article
  7. Review
  8. An Atomistic View on the Mechanism of Diatom Peptide-Guided Biomimetic Silica Formation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  9. Article
  10. Article
  11. 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

6 authors.

Johannes StroblInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Str. 38, Vienna, 109, Austria.
Fanny KozakInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Str. 38, Vienna, 109, Austria.
Meder KamalovInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Str. 38, Vienna, 109, Austria.
Daniela ReichingerInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Str. 38, Vienna, 109, Austria.
Dennis KurzbachInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Str. 38, Vienna, 109, Austria.
Christian Fw BeckerInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Str. 38, Vienna, 109, Austria.ORCID https://orcid.org/0000-0002-8890-7082

Funding

Austrian Science Fund P-33338 NAustria Wirtschaftsservice Gesellschaft mbH P1716433-WZP01European Research CouncilEuropean Union's Horizon 2020 research and innovation programme 801936
6 · The paper itself

Abstract

The most advanced materials are those found in nature. These evolutionary optimized substances provide highest efficiencies, e.g., in harvesting solar energy or providing extreme stability, and are intrinsically biocompatible. However, the mimicry of biological materials is limited to a few successful applications since there is still a lack of the tools to recreate natural materials. Herein, such means are provided based on a peptide library derived from the silaffin protein R5 that enables rational biomimetic materials design. It is now evident that biomaterials do not form via mechanisms observed in vitro. Instead, the material's function and morphology are predetermined by precursors that self-assemble in solution, often from a combination of protein and salts. These assemblies act as templates for biomaterials. The RRIL peptides used here are a small part of the silica-precipitation machinery in diatoms. By connecting RRIL motifs via varying central bi- or trifunctional residues, a library of stereoisomers is generated, which allows characterization of different template structures in the presence of phosphate ions by combining residue-resolved real-time NMR spectroscopy and molecular dynamics (MD) simulations. Understanding these templates in atomistic detail, the morphology of silica particles is controlled via manipulation of the template precursors.

Indexed as

PeptidesSilicon DioxideBiocompatible MaterialsMolecular Dynamics SimulationPeptide LibraryBiocompatible MaterialsPeptide LibraryPeptidesSilicon Dioxidebiomineralizationmolecular dynamicspeptide self-assemblysilica particlessilica precipitation

Identifiers

PMID36509953
PMCPMC11475327

What OpenQuestion holds

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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.