Evidence map›Paper›PMID 40429708›Full record

ArticleInternational journal of molecular sciences2025

Silk-Soy Alloy Materials: Influence of Silk Types (Mori, Thai, Muga, Tussah, and Eri) on the Structure, Properties, and Functionality of Insect-Plant Protein Blends (II).

Nagireddy Poluri, Christopher R Gough, Joseph Perrotta, Joseph Pinto, Maxwell Cohen, Steven Sanderlin, Christopher Velardo, Anthony Barca, Xiao Hu

Abstract read
In one paragraph

Article in International journal of molecular sciences, 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

9 authors.

Nagireddy PoluriDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.ORCID 0009-0003-6571-045X
Christopher R GoughDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.ORCID 0000-0002-1426-8150
Joseph PerrottaDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.
Joseph PintoDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.
Maxwell CohenDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.
Steven SanderlinDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.
Christopher VelardoDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.
Anthony BarcaDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.
Xiao HuDepartment of Physics and Astronomy, Rowan University, Glassboro, NJ 08028, USA.ORCID 0000-0002-2579-2820

Funding

National Science Foundation CMMI-2037097
6 · The paper itself

Abstract

Natural proteins present a sustainable and biocompatible alternative to conventional fossil fuel-derived plastics, with versatile applications in fields ranging from medicine to food packaging. Extending our previous research on silk-corn zein composites, this study utilizes soy protein-another plant protein extensively employed within biomedical applications-in conjunction with silk fibroin proteins extracted from a variety of domestic (Mori and Thai) and wild (Muga, Tussah, and Eri) silkworm species. By combining these proteins in varying ratios (0%, 10%, 25%, 50%, 75%, 90%, and 100%), silk-soy films were successfully fabricated with high miscibility. The structural and thermal stability of these films was confirmed through various characterization techniques, including Fourier transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), and scanning electron microscopy (SEM). Structural refinements were then achieved through post-water annealing treatments. After annealing, it was observed that when soy protein was introduced into both types of silk, the silks exhibited a greater amount of intermolecular and intramolecular β-sheet content. This phenomenon can be attributed to soy's intrinsic ability to self-assemble into β-sheets through electrostatic and hydrophobic interactions, which also improved the overall thermal stability and morphology of the composite films. The unique self-assembling properties of soy and its ability to promote β-sheet formation facilitate the customization of the silk source and the soy-to-silk ratio. This adaptability establishes protein-based thin films as a versatile and sustainable option for diverse applications in fields such as medicine, tissue engineering, food packaging, and beyond.

Indexed as

AlloysFibroinsInsect ProteinsSilkSoybean ProteinsAnimalsBiocompatible MaterialsBombyxCalorimetry, Differential ScanningFood PackagingSpectroscopy, Fourier Transform InfraredAlloysBiocompatible MaterialsFibroinsInsect ProteinsSilkSoybean Proteinsbiopolymercomposite filmprotein–protein interactionsecondary structuresilk fibroinsoy protein

Identifiers

PMID40429708
PMCPMC12111725

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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.