| Abstract [eng] |
Protein aggregation is associated with many neurodegenerative diseases such as Alzheimer’s, Parkinson’s, also with II type diabetes. Despite the best efforts of scientists, there is still no effective treatment for amyloid diseases. Over the past few decades, large quantities of various class inhibitors have been investigated, but none of them has successfully passed the clinical trials. Currently, one of the more promising approaches allows the inhibition of amyloid formation by small-molecule inhibitors. This approach is supported by the propensity of small molecules to specifically interact with amyloid assemblies at the molecular level and, thus, inhibit the self-assembly process. In this work, the impact of different compounds on recombinant insulin aggregation was investigated. Protein aggregation was monitored by fluorescence spectroscopy using thioflavin T (ThT) dye. A total of 31 compounds were examined, 7 of them showed weak inhibitory properties. Also it was noticed, that several inhibition paths are possible. |
