How does shear rate affect protein nanofibril formation?
Best insight from top research papers
Shear rate has been shown to have a significant effect on protein nanofibril formation . Shear flow exposure causes proteins to unfold, leading to changes in their secondary structure and the formation of β-sheets, which then aggregate to form fibrils . Shear flow accelerates the rate of fibril formation and can lead to the formation of different fibril structures depending on the shear rate applied . Increasing shear rate increases the intrinsic fibrillization rate and decreases the fibrillization time . Shear flow can also induce conformational changes in proteins, leading to the transformation of fibronectin from a compact structure to an extended fibrillar state . Shear flow can enhance the formation of protein fibrils by promoting the supply of protein monomers towards the fibril tips, but at higher shear rates, it can also cause the breakage of non-matured bonds inside the fibrils .
Answers from top 5 papers
More filters
| Papers (5) | Insight |
|---|---|
107 Citations | The paper states that the amount of protein nanofibrils formed is influenced by shear rate. At a certain shear rate, the amount of fibrils is maximal, but at higher shear rates, the amount decreases due to the breakage of non-matured bonds inside the fibrils. |
10 Citations | The paper does not provide information on how shear rate affects protein nanofibril formation. The paper focuses on the conformational changes of fibronectin (Fn) induced by shear and stainless steel. |
3 Citations | The paper states that increasing shear rate leads to an increase in the rate of protein fibrillization, but it does not specifically mention nanofibril formation. |
01 Jan 2014 2 Citations | The paper states that shear flow exposure can cause protein molecules to unfold and form fibrils. The rate of amyloid formation is directly proportional to the rate of energy dissipation in the system, suggesting that the shear rate affects protein nanofibril formation. |
20 Citations | The paper states that shear flow accelerates the rate of amyloid fibril formation by human apolipoprotein C-II. At higher shear rates, tangled ropelike structures were observed instead of twisted ribbon fibrils. |
Related Questions
What are the factors that contribute to the splitting of cellulose nanofibrils?5 answersThe splitting of cellulose nanofibrils can be influenced by various factors. Mechanical stress, such as bending, can induce molecular defects like kinks and breakages in cellulose nanofibrils, making them prone to splitting. Lytic polysaccharide monooxygenases (LPMOs) can weaken fiber cohesion and facilitate disruption, aiding in the production of nanofibrillated cellulose (NFC). Ultrasonication plays a crucial role in individualizing cellulose nanofibers, affecting their disintegration and network formation, ultimately impacting the splitting process. Additionally, the disassembly of cellulose nanofibrils can be influenced by the strength of interchain and intersheet interactions, with oxidized systems showing repulsive electrostatic interactions that weaken fibril binding. Various pretreatments like enzymatic treatments and chemical oxidations have been explored to facilitate the splitting of cellulose nanofibrils, enhancing their individualization and liberation for diverse applications.
Amyloid fibril-nanocellulose interactions and self-assembly4 answersAmyloid fibril-nanocellulose interactions and self-assembly have been studied extensively. The colloidal interactions between amyloid fibrils and nanocellulose are important for improving the mechanical properties of hybrid materials. These interactions are driven by electrostatic forces, leading to the formation of polyelectrolyte complexes that increase the elasticity of the amyloid network. Different morphologies of nanocellulose, such as cellulose nanocrystals and cellulose nanofibrils, contribute differently to the elasticity of the hybrid material. Self-assembly of amyloid-nanocellulose gels can be achieved by starting with repulsive co-dispersions and inducing attraction and cross-linking through pH changes. Understanding these interactions provides a basis for designing functional biohybrid materials.
What are the current challenges in the development of protein nanobiocomposites?5 answersThe current challenges in the development of protein nanobiocomposites include the efficient dispersion of nanoclays in biopolymer matrices to achieve homogeneous dispersion and avoid inhomogeneous nanobiocomposites with unsatisfying properties. Another challenge is the need for synergistic blending of natural and synthetic constituents to improve the structural performance of protein-based nanocomposites. Additionally, there is a need for rational integration of protein materials with synthetic organic and inorganic nanomaterials through tailored interfacial interactions to achieve synergistic enhancement in properties. Furthermore, the lack of targeting and improper biodistribution in current drug-based therapies is a major flaw that can be addressed by the development of protein nanocages for controlled drug delivery. Overall, the challenges in protein nanobiocomposite development involve achieving efficient dispersion, improving structural performance, integrating protein materials with synthetic nanomaterials, and addressing targeting and biodistribution issues in drug delivery.
How agitation in proteins cause quick fibrillation?5 answersAgitation in proteins can cause quick fibrillation by inducing unfolding and aggregation of the proteins. The mechanical shearing force generated by agitation leads to the rapid formation of amorphous aggregates in the proteins. This process is facilitated by the reduction of alpha-helical structure and the absence of beta-sheet secondary structure in the proteins. Additionally, ultrasonication, a form of agitation, has been found to trigger the spontaneous formation of fibrils in solutions of amyloidogenic proteins. The accelerating effects of ultrasonication on fibrillation suggest that cavitation microbubbles play a key role in converting the metastable state of supersaturation to the labile state, leading to spontaneous fibrillation. Overall, agitation in proteins promotes the unfolding, aggregation, and subsequent fibrillation of the proteins, potentially contributing to the development of amyloid-related diseases.
How does sonication time affect protein fibril width?4 answersSonication time has been shown to affect protein fibril width in various studies. For example, in the study by Jin et al., sonication at specific conditions resulted in a decrease in particle size of buckwheat protein isolates (BPIs) from 427.7 ± 76.7 nm to 2130.8 ± 356.2 nm. This increase in particle size indicates the formation of larger fibrils. Similarly, in the study by Maity et al., sonication induced the formation of nanofibrils in a tripeptide organogel, as observed through atomic force microscopy (AFM) and field emission scanning electron microscopy (FE-SEM). These findings suggest that longer sonication times can lead to the formation of wider protein fibrils. However, it is important to note that the specific effects of sonication time on protein fibril width may vary depending on the protein and experimental conditions used in each study.
How does sonication time affect protein fibril's radius?4 answersSonication time has been shown to affect the radius of protein fibrils. In the study by Zhu et al., sonication of walnut protein isolate resulted in a decrease in particle size, indicating the dissociation of protein aggregates. Similarly, in the study by Jin et al., sonication of buckwheat protein isolates led to an increase in particle size, suggesting the breaking of macroparticles into smaller fragments. These findings suggest that the effect of sonication time on protein fibril radius may vary depending on the specific protein and experimental conditions. Further research is needed to fully understand the relationship between sonication time and protein fibril radius.