Evidence map›Paper›PMID 34361434›Full record

ArticleMaterials (Basel, Switzerland)2021

Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface.

Pezhman Mohammadi, Fabian Zemke, Wolfgang Wagermaier, Markus B Linder

Abstract read
In one paragraph

Article in Materials (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Design and Heterologous Production of Bagworm Silk-Inspired Proteins inComputational and structural biotechnology journal · 2026
    Article
  3. Biosynthetic optical waveguide interface integration using biomimetic -Computational and structural biotechnology journal · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. Highly Hydrophobic Films of Engineered Silk Proteins by a Simple Deposition Method.Langmuir : the ACS journal of surfaces and colloids · 2023
    Article
  8. Review
  9. The complex structure ofScience advances · 2023
    Article
  10. 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

4 authors.

Pezhman MohammadiVTT Technical Research Centre of Finland Ltd., FI-02044 Espoo, Finland.ORCID 0000-0003-4593-5371
Fabian ZemkeDepartment of Biomaterials, Max Planck Institute of Colloids and Interfaces, 14476 Potsdam, Germany.
Wolfgang WagermaierDepartment of Biomaterials, Max Planck Institute of Colloids and Interfaces, 14476 Potsdam, Germany.
Markus B LinderDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, FI-02150 Espoo, Finland.

Funding

Academy of Finland through its Centres of Excellence Programme (2014-2019) 2014-2019Jenny and Antti Wihuri Foundation (Centre for Young Synbio Scientists) Centre for Young Synbio Scientists
6 · The paper itself

Abstract

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water-air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron x-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid-liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

Indexed as

coacervateconformational conversionliquid–liquid phase separationskin formationspider silkX-ray diffractionβ-sheet

Identifiers

PMID34361434
PMCPMC8348448

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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.