Evidence map›Paper›PMID 30673202›Full record

ArticleACS nano2019

Residue-Specific Solvation-Directed Thermodynamic and Kinetic Control over Peptide Self-Assembly with 1D/2D Structure Selection.

Yiyang Lin, Matthew Penna, Michael R Thomas, Jonathan P Wojciechowski, Vincent Leonardo, Ye Wang, E Thomas Pashuck, Irene Yarovsky, Molly M Stevens

Abstract read
In one paragraph

Article in ACS nano, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. 2D Assemblies Based on a Tetraphenylethylene D,L-Cyclic Peptide Scaffold.Angewandte Chemie (International ed. in English) · 2025
    Article
  3. Article
  4. Review
  5. 3,4-Ethylenedioxythiophene Hydrogels: Relating Structure and Charge Transport in Supramolecular Gels.Chemistry of materials : a publication of the American Chemical Society · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Fluorinated peptide biomaterials.Peptide science (Hoboken, N.J.) · 2021
    Article
  18. Article
  19. 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

9 authors.

Yiyang LinDepartment of Materials, Department of Bioengineering, and Institute for Biomedical Engineering , Imperial College London , Exhibition Road , London SW7 2AZ , United Kingdom.ORCID 0000-0003-2017-190X
Matthew PennaSchool of Engineering , RMIT University , Melbourne , Victoria 3001 , Australia.
Michael R ThomasDepartment of Materials, Department of Bioengineering, and Institute for Biomedical Engineering , Imperial College London , Exhibition Road , London SW7 2AZ , United Kingdom.ORCID 0000-0001-7795-9648
Jonathan P WojciechowskiDepartment of Materials, Department of Bioengineering, and Institute for Biomedical Engineering , Imperial College London , Exhibition Road , London SW7 2AZ , United Kingdom.
Vincent LeonardoDepartment of Materials, Department of Bioengineering, and Institute for Biomedical Engineering , Imperial College London , Exhibition Road , London SW7 2AZ , United Kingdom.
Ye WangDepartment of Materials, Department of Bioengineering, and Institute for Biomedical Engineering , Imperial College London , Exhibition Road , London SW7 2AZ , United Kingdom.ORCID 0000-0002-0525-1832
E Thomas PashuckDepartment of Materials, Department of Bioengineering, and Institute for Biomedical Engineering , Imperial College London , Exhibition Road , London SW7 2AZ , United Kingdom.ORCID 0000-0003-2881-4965
Irene YarovskySchool of Engineering , RMIT University , Melbourne , Victoria 3001 , Australia.ORCID 0000-0002-4033-5150
Molly M StevensSchool of Engineering , RMIT University , Melbourne , Victoria 3001 , Australia.ORCID 0000-0002-7335-266X

Funding

Biotechnology and Biological Sciences Research Council BB/L015129/1Medical Research Council MR/R015651/1Wellcome Trust
6 · The paper itself

Abstract

Understanding the self-organization and structural transformations of molecular ensembles is important to explore the complexity of biological systems. Here, we illustrate the crucial role of cosolvents and solvation effects in thermodynamic and kinetic control over peptide association into ultrathin Janus nanosheets, elongated nanobelts, and amyloid-like fibrils. We gained further insight into the solvation-directed self-assembly (SDSA) by investigating residue-specific peptide solvation using molecular dynamics modeling. We proposed the preferential solvation of the aromatic and alkyl domains on the peptide backbone and protofibril surface, which results in volume exclusion effects and restricts the peptide association between hydrophobic walls. We explored the SDSA phenomenon in a library of cosolvents (protic and aprotic), where less polar cosolvents were found to exert a stronger influence on the energetic balance at play during peptide propagation. By tailoring cosolvent polarity, we were able to achieve precise control of the peptide nanostructures with 1D/2D shape selection. We also illustrated the complexity of the SDSA system with pathway-dependent peptide aggregation, where two self-assembly states ( i.e., thermodynamic equilibrium state and kinetically trapped state) from different sample preparation methods were obtained.

Indexed as

ThermodynamicsHydrophobic and Hydrophilic InteractionsKineticsModels, MolecularPeptidesProtein ConformationSolubilityPeptides2D structuresfibrilspathway dependencepeptide solvationself-assembly

Identifiers

PMID30673202
PMCPMC6396410

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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.