Evidence map›Paper›PMID 41199803›Full record

ArticleACS sustainable chemistry & engineering2025

Amyloid-Like Self-Assembling of Black Soldier Fly Proteins and Development of Bioplastics.

Edoardo Testa, Elisa Fasoli, Paola Rizzo, Morena Casartelli, Gianluca Molla, Gianluca Tettamanti, Maurizio Galimberti

Abstract read
In one paragraph

Article in ACS sustainable chemistry & engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Edoardo TestaPolitecnico di Milano, Department of Chemistry, Materials and Chemical Engineering "G. Natta", Via Mancinelli 7, 20131 Milano, Italy.ORCID https://orcid.org/0009-0003-9180-6922
Elisa FasoliPolitecnico di Milano, Department of Chemistry, Materials and Chemical Engineering "G. Natta", Via Mancinelli 7, 20131 Milano, Italy.ORCID https://orcid.org/0000-0002-7370-993X
Paola RizzoUniversità degli Studi di Salerno, Department of Chemistry and Biology and INSTM Research Unit, Via Giovanni Paolo II 132, University of Salerno, 84084 Fisciano, Italy.ORCID https://orcid.org/0000-0002-3375-3119
Morena CasartelliUniversità degli Studi di Milano, Department of Biosciences, Via Celoria 26, 20133 Milano, Italy.
Gianluca MollaUniversità degli Studi dell'Insubria, Department of Biotechnology and Life Sciences, Via J. H. Dunant 3, 21100 Varese, Italy.
Gianluca TettamantiUniversità degli Studi dell'Insubria, Department of Biotechnology and Life Sciences, Via J. H. Dunant 3, 21100 Varese, Italy.
Maurizio GalimbertiPolitecnico di Milano, Department of Chemistry, Materials and Chemical Engineering "G. Natta", Via Mancinelli 7, 20131 Milano, Italy.ORCID https://orcid.org/0000-0001-5770-7208

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rising demand for sustainable materials has increased interest in biodegradable plastics. The black soldier fly (BSF) is a protein source characterized by the ability to thrive on organic waste, rapid development, and low environmental impact. This study shows that BSF proteins can undergo amyloid-like aggregation in alkaline environments, ultimately leading to amyloid fibrils suitable as reinforcing nanofillers for bioplastic films. The fibrillization process was monitored through Thioflavin-T (ThT) fluorescence assay and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The fibrils' structure was studied by means of transmission electron microscopy (TEM) and one-dimensional/two-dimensional (1D/2D) X-ray diffraction (XRD) analyses performed on films obtained by casting. Bioplastic films were prepared by blending fibrillizated BSF proteins with poly-(vinyl alcohol) (PVOH) and glycerol. They exhibited thermal weldability and mechanical and gas barrier properties in line with those of the traditional oil- and biobased plastics used for packaging applications. Due to the current technological interest in BSF as a bioconverter of organic matter, the BSF protein-based materials presented in this work not only could help in mitigating the pressure arising from the accumulation of nonbiodegradable plastics but also provide tangible evidence about the valorization of municipal organic waste.

Indexed as

amyloid fibrilsbioplasticshermetia illucenspackagingproteins

Identifiers

PMID41199803
PMCPMC12588267

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.