Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide

May 22, 2018

Title

Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide

Author

Xiaocui Fang, Maryam Yousaf, Qunxing Huang, Yanlian Yang, Chen Wang

Year

2018

Journal

Scientific Reports

Abstract

The oligomerization and fibrillation of human islet amyloid polypeptide (hIAPP) play a central role in the pathogenesis of type 2 diabetes. Strategies for remodelling the formation of hIAPP oligomers and fibrils have promising application potential in type 2 diabetes therapy. Herein, we demonstrated that PEG-PE micelle could inhibit hIAPP oligomerization and fibrillation through blocking the hydrophobic interaction and the conformational change from random coil to β-sheet structures of hIAPP. In addition, we also found that PEG-PE micelle could remodel the preformed hIAPP fibrils allowing the formation of short fibrils and co-aggregates. Taken together, PEG-PE micelle could rescue hIAPP-induced cytotoxicity by decreasing the content of hIAPP oligomers and fibrils that are related to the oxidative stress and cell membrane permeability. This study could be beneficial for the design and development of antiamyloidogenic agents.

Instrument

J-810

Keywords

Circular dichroism, Secondary structure, Vesicle interactions, Aggregation, Biochemistry