Investigation of the kinetics of insulin amyloid fibrils formation

Сулацкая, А. И.; Volova, E A; Комиссарчик, Я.Ю.; Snigirevskaia, E S; Маскевич, А. А.; Дробченко, Е. А.; Kuznetsova, Irina M.; Turoverov, Konstantin K.

doi:10.1134/s1990519x14020114

Cited by 10 publications

(4 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this range, ThT binding would also be closer to saturation and thus less variable with time. Similar arguments have been put forward by Sulatskaya et al 22 This conclusion is consistent with the demonstration of linearity in the ThT assay for Aβ(1− 42) aggregation in the presence of excess ThT in the Supporting Information of ref 6 and also with our previous study of insulin fibril formation. 10 Altogether, our work highlights the complexity of ThT photophysics and suggests that these effects should be taken into careful consideration in the design and analysis of in vitro experimental data.…”

supporting

confidence: 92%

Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

et al. 2017

View full text Add to dashboard Cite

Thioflavin-T binds to and detects amyloid fibrils via fluorescence enhancement. Using a combination of linear dichroism and fluorescence spectroscopies, we report that the relation between the emission intensity and binding of thioflavin-T to insulin fibrils is nonlinear and discuss this in relation to its use in kinetic assays. We demonstrate, from fluorescence lifetime recordings, that the nonlinearity is due to thioflavin-T being sensitive to self-quenching. In addition, thioflavin-T can induce fibril compaction but not alter fibril structure. Our work underscores the photophysical complexity of thioflavin-T and the necessity of calibrating the linear range of its emission response for quantitative in vitro studies.

show abstract

supporting

confidence: 92%

Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

et al. 2017

View full text Add to dashboard Cite

show abstract

“…26 Additionally, the possibility of formation of intermediates such as protofibrils and oligomers cannot be ignored. 27 There are 20 homologous proteins and a few associated proteins such as Ab1-40, 28 lysozymes, 29 and insulin, 30 which are known to form amyloid fibrils that trigger incurable diseases such as Parkinson's disease. 31 Amyloid fibrils comprise 3-6 filaments that change form when the unfolded monomers are assembled into oligomers, followed by transformation into the metastable b-sheet conformation and subsequently into b-sheet rich structures.…”

Section: Kazuaki Matsumuramentioning

confidence: 99%

Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials

et al. 2021

View full text Add to dashboard Cite

show abstract

“…It has been shown that aggregation and fibrillation of insulin are also produced during production, storage, and delivery of insulin based drugs [ 127 ]. In addition, insulin amyloid fibrils were also found in type 2 diabetic patients after a single or repeated subcutaneous injection of insulin [ 128 ]. There was an interesting data demonstrating that insulin fibrillation induced cytotoxicity in the pheochromocytoma PC12 and human neuroblastoma SH-SY5Y cell lines [ 129 ].…”

Section: Potential Mechanisms Of Action Of Cinnamic Acid and Its Dmentioning

confidence: 99%

Cinnamic Acid and Its Derivatives: Mechanisms for Prevention and Management of Diabetes and Its Complications

2017

View full text Add to dashboard Cite

With recent insight into the development of dietary supplements and functional foods, search of effective phytochemical compounds and their mechanisms involved in prevention and management of diabetes and its complications are now being assessed. Cinnamic acid and its derivatives occur naturally in high levels of plant-based foods. Among various biological activities, cinnamic acid and its derivatives are associated with a beneficial influence on diabetes and its complications. The aim of the review is to summarize the potential mechanisms of these compounds for prevention and management of diabetes and its complications. Based on several in vitro studies and animal models, cinnamic acid and its derivatives act on different mechanism of actions, including stimulation of insulin secretion, improvement of pancreatic β-cell functionality, inhibition of hepatic gluconeogenesis, enhanced glucose uptake, increased insulin signaling pathway, delay of carbohydrate digestion and glucose absorption, and inhibition of protein glycation and insulin fibrillation. However, due to the limited intestinal absorption being a result of low bioavailability of cinnamic acid and its derivatives, current improvement efforts with entrapping into solid and liquid particles are highlighted. Further human clinical studies are needed to clarify the effects of cinnamic acid and its derivatives in diabetic patients.

show abstract

Investigation of the kinetics of insulin amyloid fibrils formation

Cited by 10 publications

References 25 publications

Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials

Cinnamic Acid and Its Derivatives: Mechanisms for Prevention and Management of Diabetes and Its Complications

Contact Info

Product

Resources

About