Interaction of Human Amylin with Phosphatidylcholine and Phosphatidylserine Membranes

Abstract

We studied the interaction of human amylin with dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylserine vesicles using differential scanning calorimetry, circular dichroism and molecular modelling. The results suggest that inappropriate insertion of amylin into the hydrophobic core of a lipid bilayer could hinder the secretion of amylin from pancreatic β-cells.

Keywords:

• amylin
• circular dicroism
• differential scanning calorimetry
• lipid bilayer
• molecular modeling

Acknowledgments

This research was financially supported by MIUR (FIRB [Ncirc] RBNE03PX83, PRIN 2005035119002) and University of Catania.

Notes

^aInitially hIAPP adopts an α-helix conformation, but rapidly converts into β-sheet structure [13].