ArticleJournal of biomedical physics & engineering2020
Study of Nanofibrils Formation of Fibroin Protein in Specific Thermal and Acidity Conditions.
Article in Journal of biomedical physics & engineering, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Silk Fibroin Aggregates at the Air-Water Interface: Amyloid-like Fibrils vs. Self-Assembled Networks.International journal of molecular sciences · 2026Article
- Formation and Physicochemical Properties of Freeze-Dried Amyloid-Like Fibrils From Pinto Bean Protein: Amyloid-Like Fibrils From Pinto Bean Protein.International journal of analytical chemistry · 2024Article
- Application of Nanotechnology for Sensitive Detection of Low-Abundance Single-Nucleotide Variations in Genomic DNA: A Review.Nanomaterials (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAmyloid fibrils are insoluble arranged aggregates of proteins that are fibrillar in structure and related to many diseases (at least 20 types of illnesses) and also create many pathologic conditions. Therefore understanding the circumstance of fibril formation is very important.
objectivesThis study aims to work on fibrillar structure formation of fibroin (as a model protein). MATERIAL AND
methodsIn this experimental study, fibroin was extracted from bombyx mori silk cocoon, and the concentration was obtained by Bradford method. The protein was incubated in a wide range of times (0 min to 7 days) in specific acidity and thermal conditions (pH=1.6, T=70 °C). The assays of UV-vis spectroscopy with congo red, field emission scanning electron microscopy, transmission electron microscopy, atomic force microscopy and circular dichroism spectroscopy were employed to monitor the fibrillation process.
resultsFibroin assemblies were formed upon the process of aggregation and fibril formation with a variety of morphology ranging from nanoparticles to elongated fibrils.
conclusionThe results showed progressive pathway of fibril formation.
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Registered trials
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