特定热条件和酸度条件下丝素蛋白纳米纤维形成的研究
Study of Nanofibrils Formation of Fibroin Protein in Specific Thermal and Acidity Conditions.
作者信息
M Ahrami, M Khatami, H Heli
机构信息
MSc, Department of Nanomedicine, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences, Shiraz, Iran.
MSc, Nanomedicine and Nanobiology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran.
出版信息
J Biomed Phys Eng. 2020 Feb 1;10(1):39-50. doi: 10.31661/jbpe.v0i0.1092. eCollection 2020 Feb.
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
This study aims to work on fibrillar structure formation of fibroin (as a model protein).
MATERIAL AND 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
Fibroin assemblies were formed upon the process of aggregation and fibril formation with a variety of morphology ranging from nanoparticles to elongated fibrils.
CONCLUSION
The results showed progressive pathway of fibril formation.
背景
淀粉样纤维是蛋白质的不溶性排列聚集体，其结构呈纤维状，与许多疾病（至少20种疾病）相关，也会引发许多病理状况。因此，了解纤维形成的情况非常重要。
目的
本研究旨在研究丝素蛋白（作为一种模型蛋白）的纤维状结构形成。
材料与方法
在本实验研究中，从家蚕茧中提取丝素蛋白，并通过Bradford法测定其浓度。将该蛋白在特定的酸度和热条件（pH = 1.6，T = 70°C）下孵育不同时间（0分钟至7天）。采用刚果红紫外可见光谱法、场发射扫描电子显微镜、透射电子显微镜、原子力显微镜和圆二色光谱法监测纤维化过程。
结果
在聚集和纤维形成过程中形成了丝素蛋白聚集体，其形态多样，从纳米颗粒到细长纤维不等。
结论
结果显示了纤维形成的渐进途径。
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