Evidence map›Paper›PMID 28084315›Full record

ArticleNature communications2017

A minimal length rigid helical peptide motif allows rational design of modular surfactants.

Sudipta Mondal, Maxim Varenik, Daniel Nir Bloch, Yoav Atsmon-Raz, Guy Jacoby, Lihi Adler-Abramovich, Linda J W Shimon, Roy Beck, Yifat Miller, Oren Regev and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Assessment of the MARTINI 3 Performance for Short Peptide Self-Assembly.Journal of chemical theory and computation · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Progress in synthesizing protocells.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  16. Review
  17. Article
  18. Reductionist Approach in Peptide-Based Nanotechnology.Annual review of biochemistry · 2018
    Review
  19. Review
  20. Review
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.

Sudipta MondalDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Maxim VarenikDepartment of Chemical Engineering, Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel.
Daniel Nir BlochDepartment of Chemistry, Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel.
Yoav Atsmon-RazDepartment of Chemistry, Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel.ORCID 0000-0001-6476-9845
Guy JacobyThe Raymond and Beverly Sackler School of Physics and Astronomy, Tel Aviv University, Tel Aviv 69978, Israel.
Lihi Adler-AbramovichDepartment of Oral Biology, The Goldschleger School of Dental Medicine, Tel Aviv University, Tel Aviv 69978, Israel.
Linda J W ShimonDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot 76100, Israel.
Roy BeckThe Raymond and Beverly Sackler School of Physics and Astronomy, Tel Aviv University, Tel Aviv 69978, Israel.ORCID 0000-0003-3121-4530
Yifat MillerDepartment of Chemistry, Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel.
Oren RegevDepartment of Chemical Engineering, Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel.
Ehud GazitDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.

Funding

European Research Council 694426
6 · The paper itself

Abstract

Extensive work has been invested in the design of bio-inspired peptide emulsifiers. Yet, none of the formulated surfactants were based on the utilization of the robust conformation and self-assembly tendencies presented by the hydrophobins, which exhibited highest surface activity among all known proteins. Here we show that a minimalist design scheme could be employed to fabricate rigid helical peptides to mimic the rigid conformation and the helical amphipathic organization. These designer building blocks, containing natural non-coded α-aminoisobutyric acid (Aib), form superhelical assemblies as confirmed by crystallography and microscopy. The peptide sequence is amenable to structural modularity and provides the highest stable emulsions reported so far for peptide and protein emulsifiers. Moreover, we establish the ability of short peptides to perform the dual functions of emulsifiers and thickeners, a feature that typically requires synergistic effects of surfactants and polysaccharides. This work provides a different paradigm for the molecular engineering of bioemulsifiers.

Indexed as

Amino Acid SequenceAminoisobutyric AcidsCrystallographyModels, MolecularMolecular Sequence DataPeptidesProtein ConformationProteinsSurface-Active Agents2-aminoisobutyric acidAminoisobutyric AcidsPeptidesProteinsSurface-Active Agents

Identifiers

PMID28084315
PMCPMC5241864

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.