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Studying the effects of silymarin on in vitro formation of α-amylase amyloid aggregate
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Hoda Jahangiri   , Shahrbanoo Oryan , Parichehre Yaghmaii , Azade Ebrahim Habibi , Maryam Nikkhah |
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Abstract: (244 Views) |
Introduction: The accumulation of proteins and the formation of protein amyloids are the main causes of diabetes, Parkinson's, and Alzheimer's disease. Flavonoids derived from plants would to be effective in inhibiting the formation of this process. Thus, the purpose of this study is to investigate whether silymarin inhibits the formation of amyloid amylase.
Methods and Materials: As a means of inducing amyloid accumulations and checking all possible conditions, five different modes of four variables were examined, including protein concentration, pH, temperature, and incubation time. There were three concentrations of protein used, one, two, and three mg/ml. A pH of 2, 7 and 10 was used. Having established the most favorable conditions for the formation of amylase amyloid fibrils, the next experiment examined the effects of silymarin on preventing their formation. This was accomplished by selecting concentrations of 0.1, 0.5, 1, 2 and 5 mM and incubating them at 37°C for eight days. In order to investigate fibril formation, ThT fluorescence assay, Congo red color spectroscopy and transmission electron microscopy (TEM) were used.
Results: The preliminary results showed that among the different treatments, the best condition for fibril formation was protein concentration of 3 mg/ml, which was chosen for further research. However, in protein samples incubated in the presence of the 5 mg/ml of silymarin, amyloid fibrils were absent and amorphous protein structure were observed. The results obtained from ThT fluorescence and Congo red color spectroscopy also confirmed the protective effect of silymarin in preventing the formation of amylase fibrils.
Conclutions: Based on these findings, it can be concluded that silymarin effectively suppresses the aggregation of amorphous amylase caused by heat and pH. Therefore, silymarin may be a promising drug for the control of complications caused by damage related to amyloid fibrils in the continuation of therapeutic research.
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| Keywords: amylase, amyloid fibrils, Silymarins |
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Full-Text [PDF 381 kb]
(37 Downloads)
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Type of Study: Research |
Subject:
General
Received: 2024/02/2 | Accepted: 2023/08/23 | Published: 2023/08/23
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