Study of Nanofibrils Formation of Fibroin Protein in Specific Thermal and Acidity Conditions

Abstract

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.

In vitro and in vivo anticancer effect of pH-responsive paclitaxel-loaded niosomes

“…Nanomedicine is the field of science that deals with organic applications of medicine at the nano-scale level [13][14][15][16][17]. It primarily addresses finding, anticipating, and treating sickness, as well as using nanotechnology to assist in controlling human frameworks at the cellular level [18][19][20][21][22][23][24][25]. For example, niosomes and liposomes have a similar shape, but instead of phospholipids, nonionic surfactants are used for noisome preparation.…”

Silk Fibroin Self-Assembly at the Air–Water Interface

“…The increase of protein concentration leads to an increase of micelles and subsequent transition to a gel phase [28]. This self-assembly is a complex process and there is a large set of parameters affecting it: the solution's ionic strength, pH, temperature, and hydrodynamic shear forces [24,[29][30][31][32][33][34]. When the pH decreases from 6.8 to 4.8, the secondary structure of aggregates can change due to the formation of β-sheets [33].…”

“…This self-assembly is a complex process and there is a large set of parameters affecting it: the solution's ionic strength, pH, temperature, and hydrodynamic shear forces [24,[29][30][31][32][33][34]. When the pH decreases from 6.8 to 4.8, the secondary structure of aggregates can change due to the formation of β-sheets [33]. In this case, the micelles are transformed into fibrils [27,33].…”

“…When the pH decreases from 6.8 to 4.8, the secondary structure of aggregates can change due to the formation of β-sheets [33]. In this case, the micelles are transformed into fibrils [27,33]. The addition of small seeds of fibrillar aggregates and a temperature increase can lead to the formation of amyloid SF structures [30][31][32][33][34].…”

Application of Nanotechnology for Sensitive Detection of Low-Abundance Single-Nucleotide Variations in Genomic DNA: A Review

“…As a burgeoning field, nanotechnology uses nanoscale materials for many biomedical applications, including gene therapy drug delivery, tissue engineering, etc. [ 26 , 27 , 28 , 29 , 30 ]. Controlling the size of nanomaterials contributes to the emergence of new microscopic properties [ 31 , 32 , 33 ].…”