Study of Nanofibrils Formation of Fibroin Protein in Specific Thermal and Acidity Conditions.
Amyloid Fibrils
Circular Dichroism
Fibroins
Microscopy, Electron, Scanning
Silk Fibroin
Transmission Electron Microscopy
Journal
Journal of biomedical physics & engineering
ISSN: 2251-7200
Titre abrégé: J Biomed Phys Eng
Pays: Iran
ID NLM: 101589641
Informations de publication
Date de publication:
Feb 2020
Feb 2020
Historique:
received:
22
12
2018
accepted:
28
01
2019
entrez:
12
3
2020
pubmed:
12
3
2020
medline:
12
3
2020
Statut:
epublish
Résumé
Amyloid 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. This study aims to work on fibrillar structure formation of fibroin (as a model protein). In 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. Fibroin assemblies were formed upon the process of aggregation and fibril formation with a variety of morphology ranging from nanoparticles to elongated fibrils. The results showed progressive pathway of fibril formation.
Sections du résumé
BACKGROUND
BACKGROUND
Amyloid 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.
OBJECTIVES
OBJECTIVE
This study aims to work on fibrillar structure formation of fibroin (as a model protein).
MATERIAL AND METHODS
METHODS
In 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.
RESULTS
RESULTS
Fibroin assemblies were formed upon the process of aggregation and fibril formation with a variety of morphology ranging from nanoparticles to elongated fibrils.
CONCLUSION
CONCLUSIONS
The results showed progressive pathway of fibril formation.
Identifiants
pubmed: 32158710
doi: 10.31661/jbpe.v0i0.1092
pii: JBPE-10-1
pmc: PMC7036415
doi:
Types de publication
Journal Article
Langues
eng
Pagination
39-50Informations de copyright
Copyright: © 2020: Journal of Biomedical Physics and Engineering.
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