Title
Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide
Author
Biao Cheng, Hao Gong, Xiaochao Li, Yue Sun, Xin Zhang, Hong Chen, Xinran Liu, Ling Zheng, Kun Huang
Year
2012
Journal
Biochemical and Biophysical Research Communications
Abstract
In type 2 diabetes mellitus (T2DM), misfolded human islet amyloid polypeptide (hIAPP) forms amyloid deposits in pancreatic islets. These amyloid deposits contribute to the dysfunction of β-cells and the loss of β-cell mass in T2DM patients. Inhibition of hIAPP fibrillization has been regarded as a potential therapeutic approach for T2DM. Silibinin, a major active flavonoid extracted from herb milk thistle (Silybum marianum), has been used for centuries to treat diabetes in Asia and Europe with unclear mechanisms. In this study, we tested whether silibinin has any effect on the amyloidogenicity of hIAPP. Our results provide first evidence that silibinin inhibits hIAPP fibrillization via suppressing the toxic oligomerization of hIAPP and enhances the viability of pancreatic β-cells, therefore silibinin may serve as a potential therapeutic agent for T2DM.
Instrument
J-810
Keywords
Circular dichroism, Secondary structure, Aggregation, Biochemistry, Pharmaceutical