Ascorbic acid inhibits human insulin aggregation and protects against amyloid induced cytotoxicity

作者：Alam Parvez; Beg Ayesha Zainab; Siddiqi Mohammad Khursheed; Chaturvedi Sunlit Kumar; Rajpoot Ravi Kant; Ajmal Mohd Rehan; Zaman Masihuz; Abdelhameed Ali S; Khan Rizwan Hasan

来源：Archives of Biochemistry and Biophysics, 2017, 621: 54-62.

DOI：10.1016/j.abb.2017.04.005

• Amyloids
• ThT binding
• Beta sheet structure
• Cell cytotoxicity

Protein aggregation into oligomers and fibrils are associated with many human pathophysiologies. Compounds that modulate protein aggregation and interact with preformed fibrils and convert them to less toxic species, expect to serve as promising drug candidates and aid to the drug development efforts against aggregation diseases. In present study, the kinetics of amyloid fibril formation by human insulin (HI) and the anti-amyloidogenic activity of ascorbic acid (AA) were investigated by employing various spectroscopic, imaging and computational approaches. We demonstrate that ascorbic acid significantly inhibits the fibrillation of HI in a dose-dependent manner. Interestingly ascorbic acid destabilise the preformed amyloid fibrils and protects human neuroblastoma cell line (SH- SY5Y) against amyloid induced cytotoxicity. The present data signifies the role of ascorbic acid that can serve as potential molecule in preventing human insulin aggregation and associated pathophysiologies.

• 出版日期2017-5-1