Evidence map›Paper›PMID 32894630›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Co-Assembly between Fmoc Diphenylalanine and Diphenylalanine within a 3D Fibrous Viscous Network Confers Atypical Curvature and Branching.

Priyadarshi Chakraborty, Yiming Tang, Tom Guterman, Zohar A Arnon, Yifei Yao, Guanghong Wei, Ehud Gazit

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. 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. Article
  2. Protopeptide backbone affects assembly in aqueous solutions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Phenylalanine-Based Amphiphilic Self-Assembled Materials: Gels or Crystals?Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Polypyrrole-Stabilized Polypeptide for Eco-Friendly Supercapacitors.International journal of molecular sciences · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. 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

7 authors.

Priyadarshi ChakrabortySchool of Molecular Cell Biology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, 6997801, Israel.
Yiming TangDepartment of Physics, State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (MOE), Fudan University, Shanghai, 200433, People's Republic of China.
Tom GutermanSchool of Molecular Cell Biology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, 6997801, Israel.
Zohar A ArnonSchool of Molecular Cell Biology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, 6997801, Israel.
Yifei YaoDepartment of Physics, State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (MOE), Fudan University, Shanghai, 200433, People's Republic of China.
Guanghong WeiDepartment of Physics, State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (MOE), Fudan University, Shanghai, 200433, People's Republic of China.
Ehud GazitSchool of Molecular Cell Biology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, 6997801, Israel.ORCID 0000-0001-5764-1720

Funding

European Research Council 694426
6 · The paper itself

Abstract

Supramolecular polymer co-assembly is a useful approach to modulate peptide nanostructures. However, the co-assembly scenario where one of the peptide building blocks simultaneously forms a hydrogel is yet to be studied. Herein, we investigate the co-assembly formation of diphenylalanine (FF), and Fmoc-diphenylalanine (FmocFF) within the 3D network of FmocFF hydrogel. The overlapping peptide sequence between the two building blocks leads to their co-assembly within the gel state modulating the nature of the FF crystals. We observe the formation of branched microcrystalline aggregates with an atypical curvature, in contrast to the FF assemblies obtained from aqueous solution. Optical microscopy reveal the sigmoidal kinetic growth profile of these aggregates. Microfluidics and ToF-SIMS experiments exhibit the presence of co-assembled structures of FF and FmocFF in the crystalline aggregates. Molecular dynamics simulation was used to decipher the mechanism of co-assembly formation.

Indexed as

aggregationamyloidsco-assemblycrystallizationdiphenylalanine

Identifiers

PMID32894630
PMCPMC7616930

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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.