Evidence map›Paper›PMID 39023515›Full record

ArticleChemSusChem2025

Fine Structural Analysis of Degummed Fibroin Fibers Reveals Its Superior Mechanical Capabilities.

D Eliaz, I Kellersztein, M E Miali, D Benyamin, O Brookstein, C Daraio, H D Wagner, U Raviv, U Shimanovich

Abstract read
In one paragraph

Article in ChemSusChem, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
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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.

D EliazDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, 7610001, Rehovot, Israel.
I KellerszteinDivision of Engineering and Applied Science, California Institute of Technology, Pasadena, California, 91125, USA.ORCID 0000-0002-8838-818X
M E MialiDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, 7610001, Rehovot, Israel.
D BenyaminInstitute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, 9190401, Jerusalem, Israel.
O BrooksteinDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, 7610001, Rehovot, Israel.
C DaraioDivision of Engineering and Applied Science, California Institute of Technology, Pasadena, California, 91125, USA.ORCID 0000-0001-5296-4440
H D WagnerDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, 7610001, Rehovot, Israel.ORCID 0000-0002-0741-2169
U RavivInstitute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, 9190401, Jerusalem, Israel.ORCID 0000-0001-5992-9437
U ShimanovichDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, 7610001, Rehovot, Israel.ORCID 0000-0003-3148-0142

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bombyx mori silk fibroin fibers constitute a class of protein building blocks capable of functionalization and reprocessing into various material formats. The properties of these fibers are typically affected by the intense thermal treatments needed to remove the sericin gum coating layer. Additionally, their mechanical characteristics are often misinterpreted by assuming the asymmetrical cross-sectional area (CSA) as a perfect circle. The thermal treatments impact not only the mechanics of the degummed fibroin fibers, but also the structural configuration of the resolubilized protein, thereby limiting the performance of the resulting silk-based materials. To mitigate these limitations, we explored varying alkali conditions at low temperatures for surface treatment, effectively removing the sericin gum layer while preserving the molecular structure of the fibroin protein, thus, maintaining the hierarchical integrity of the exposed fibroin microfiber core. The precise determination of the initial CSA of the asymmetrical silk fibers led to a comprehensive analysis of their mechanical properties. Our findings indicate that the alkali surface treatment raised the Young's modulus and tensile strength, by increasing the extent of the fibers' crystallinity, by approximately 40 % and 50 %, respectively, without compromising their strain. Furthermore, we have shown that this treatment facilitated further production of high-purity soluble silk protein with rheological and self-assembly characteristics comparable to those of native silk feedstock, initially stored in the animal's silk gland. The developed approaches benefits both the development of silk-based materials with tailored properties and the proper mechanical characterization of asymmetrical fibrous biological materials made of natural building blocks.

Indexed as

BombyxFibroinsAnimalsMechanical PhenomenaTensile StrengthFibroinsDegummingMechanical propertiesProtein self-assemblySilk fibersβ-sheet conformation

Identifiers

PMID39023515
PMCPMC11696198

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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.